Hemoglobin subunit alpha

Human hemoglobin protein
HBA1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1A00, 1A01, 1A0U, 1A0Z, 1A3N, 1A3O, 1A9W, 1ABW, 1ABY, 1AJ9, 1B86, 1BAB, 1BBB, 1BIJ, 1BUW, 1BZ0, 1BZ1, 1BZZ, 1C7B, 1C7C, 1C7D, 1CLS, 1CMY, 1COH, 1DKE, 1DXT, 1DXU, 1DXV, 1FDH, 1FN3, 1G9V, 1GBU, 1GBV, 1GLI, 1GZX, 1HAB, 1HAC, 1HBA, 1HBB, 1HBS, 1HCO, 1HDB, 1HGA, 1HGB, 1HGC, 1HHO, 1IRD, 1J3Y, 1J3Z, 1J40, 1J41, 1J7S, 1J7W, 1J7Y, 1JY7, 1K0Y, 1K1K, 1KD2, 1LFL, 1LFQ, 1LFT, 1LFV, 1LFY, 1LFZ, 1LJW, 1M9P, 1MKO, 1NEJ, 1NIH, 1NQP, 1O1I, 1O1J, 1O1K, 1O1L, 1O1M, 1O1N, 1O1O, 1O1P, 1QI8, 1QSH, 1QSI, 1QXD, 1QXE, 1R1X, 1R1Y, 1RPS, 1RQ3, 1RQ4, 1RQA, 1RVW, 1SDK, 1SDL, 1SHR, 1SI4, 1THB, 1UIW, 1VWT, 1XXT, 1XY0, 1XYE, 1XZ2, 1XZ4, 1XZ5, 1XZ7, 1XZU, 1XZV, 1Y01, 1Y09, 1Y0A, 1Y0C, 1Y0D, 1Y0T, 1Y0W, 1Y22, 1Y2Z, 1Y31, 1Y35, 1Y45, 1Y46, 1Y4B, 1Y4F, 1Y4G, 1Y4P, 1Y4Q, 1Y4R, 1Y4V, 1Y5F, 1Y5J, 1Y5K, 1Y7C, 1Y7D, 1Y7G, 1Y7Z, 1Y83, 1Y85, 1Y8W, 1YDZ, 1YE0, 1YE1, 1YE2, 1YEN, 1YEO, 1YEQ, 1YEU, 1YEV, 1YFF, 1YG5, 1YGD, 1YGF, 1YH9, 1YHE, 1YHR, 1YIE, 1YIH, 1YVQ, 1YVT, 1YZI, 1Z8U, 2D5Z, 2D60, 2DN1, 2DN2, 2DN3, 2DXM, 2H35, 2HBC, 2HBD, 2HBE, 2HBF, 2HBS, 2HCO, 2HHD, 2HHE, 2M6Z, 2W6V, 2W72, 2YRS, 3B75, 3D17, 3D7O, 3DUT, 3HXN, 3IA3, 3IC0, 3IC2, 3KMF, 3NL7, 3NMM, 3ODQ, 3ONZ, 3OO4, 3OO5, 3OVU, 3P5Q, 3QJB, 3QJC, 3QJD, 3QJE, 3R5I, 3S48, 3S65, 3S66, 3SZK, 3WCP, 3WHM, 4FC3, 4HHB, 4IJ2, 4L7Y, 4M4A, 4M4B, 4MQC, 4MQG, 4MQH, 4MQI, 4MQJ, 4MQK, 4N7N, 4N7O, 4N7P, 4N8T, 4NI0, 4NI1, 4ROL, 4ROM, 4WJG, 4X0L, 4XS0, 6HBW, 5E29, 5E6E, 5EE4, 5HU6, 5JDO, 5KDQ, 5E83,%%s1Y01, 1Z8U, 1BZ1

Identifiers
AliasesHBA1, HBA-T3, HBH, hemoglobin subunit alpha 1, METHBA, ECYT7
External IDsOMIM: 141800 MGI: 96015 HomoloGene: 469 GeneCards: HBA1
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)[1]
Chromosome 16 (human)
Genomic location for HBA1
Genomic location for HBA1
Band16p13.3Start176,680 bp[1]
End177,522 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for HBA1
Genomic location for HBA1
Band11 A4|11 18.86 cMStart32,233,511 bp[2]
End32,234,465 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • blood

  • bone marrow

  • bone marrow cells

  • placenta

  • spleen

  • ganglionic eminence

  • temporal lobe

  • amygdala

  • upper lobe of left lung
Top expressed in
  • bone marrow

  • spleen

  • lung

  • yolk sac

  • neural tube

  • mesencephalon

  • heart

  • cerebellar cortex

  • zone of skin

  • adrenal gland
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • iron ion binding
  • oxygen binding
  • peroxidase activity
  • oxygen carrier activity
  • metal ion binding
  • protein binding
  • heme binding
  • haptoglobin binding
  • organic acid binding
Cellular component
  • cytosol
  • endocytic vesicle lumen
  • blood microparticle
  • membrane
  • extracellular region
  • cytosolic small ribosomal subunit
  • hemoglobin complex
  • extracellular exosome
  • haptoglobin-hemoglobin complex
  • extracellular space
Biological process
  • positive regulation of cell death
  • protein heterooligomerization
  • oxygen transport
  • receptor-mediated endocytosis
  • bicarbonate transport
  • hydrogen peroxide catabolic process
  • response to hydrogen peroxide
  • cellular oxidant detoxification
  • transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3039

15122

Ensembl

ENSG00000206172

ENSMUSG00000069919

UniProt

P69905

Q91VB8

RefSeq (mRNA)

NM_000558

NM_008218

RefSeq (protein)

NP_000508
NP_000508.1
NP_000549.1

NP_001077424

Location (UCSC)Chr 16: 0.18 – 0.18 MbChr 11: 32.23 – 32.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Hemoglobin subunit alpha, Hemoglobin, alpha 1,[5] is a hemoglobin protein that in humans is encoded by the HBA1 gene.[6]

Gene

The human alpha globin gene cluster located on chromosome 16 spans about 30 kb and includes seven loci: 5'- zeta - pseudozeta - mu - pseudoalpha-1 - alpha-2 - alpha-1 - theta - 3'. The alpha-2 (HBA2) and alpha-1 (HBA1; this gene) coding sequences are identical. These genes differ slightly over the 5' untranslated regions and the introns, but they differ significantly over the 3' untranslated regions.[6]

Protein

Two alpha chains plus two beta chains constitute HbA, which in normal adult life accounts for about 97% of the total hemoglobin; alpha chains combine with delta chains to constitute HbA-2, which with fetal hemoglobin (HbF), composed of alpha and gamma chains, make up the remaining 3% of adult hemoglobin.[6]

Clinical significance

Alpha thalassemias result from deletions of each of the alpha genes as well as deletions of both HBA2 and HBA1; some nondeletion alpha thalassemias have also been reported.[6]

Interactions

Hemoglobin subunit alpha has been shown to interact with hemoglobin subunit beta (HBB).[7][8]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000206172 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000069919 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "HBA1 gene: MedlinePlus Genetics".
  6. ^ a b c d "Entrez Gene: HBA1 hemoglobin, alpha 1".
  7. ^ Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  8. ^ Shaanan B (November 1983). "Structure of human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. 171 (1): 31–59. doi:10.1016/S0022-2836(83)80313-1. PMID 6644819.

Further reading

  • Turbpaiboon C, Svasti S, Sawangareetakul P, et al. (2002). "Hb Siam [alpha15(A13)Gly→Arg (alpha1) (GGT→CGT)] is a typical alpha chain hemoglobinopathy without an alpha-thalassemic effect". Hemoglobin. 26 (1): 77–81. doi:10.1081/HEM-120002944. PMID 11939517. S2CID 85035930.
  • Yalçin A, Avcu F, Beyan C, et al. (1995). "A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala→Glu]". Hemoglobin. 18 (6): 433–5. doi:10.3109/03630269409045775. PMID 7713747.
  • Giardina B, Messana I, Scatena R, Castagnola M (1995). "The multiple functions of hemoglobin". Crit. Rev. Biochem. Mol. Biol. 30 (3): 165–96. doi:10.3109/10409239509085142. PMID 7555018.
  • Higgs DR, Vickers MA, Wilkie AO, et al. (1989). "A review of the molecular genetics of the human alpha-globin gene cluster". Blood. 73 (5): 1081–104. doi:10.1182/blood.V73.5.1081.1081. PMID 2649166.
  • Schillirò G, Russo-Mancuso G, Dibenedetto SP, et al. (1992). "Six rare hemoglobin variants found in Sicily". Hemoglobin. 15 (5): 431–7. doi:10.3109/03630269108998862. PMID 1802885.
  • Vafa M, Troye-Blomberg M, Anchang J, et al. (2008). "Multiplicity of Plasmodium falciparum infection in asymptomatic children in Senegal: relation to transmission, age and erythrocyte variants". Malar. J. 7: 17. doi:10.1186/1475-2875-7-17. PMC 2267475. PMID 18215251.
  • Datta P, Chakrabarty S, Chakrabarty A, Chakrabarti A (2008). "Membrane interactions of hemoglobin variants, HbA, HbE, HbF and globin subunits of HbA: effects of aminophospholipids and cholesterol". Biochim. Biophys. Acta. 1778 (1): 1–9. doi:10.1016/j.bbamem.2007.08.019. PMID 17916326.
  • Taylor JG, Ackah D, Cobb C, et al. (2008). "Mutations and polymorphisms in hemoglobin genes and the risk of pulmonary hypertension and death in sickle cell disease". Am. J. Hematol. 83 (1): 6–14. doi:10.1002/ajh.21035. PMC 3509176. PMID 17724704.
  • Sahu SC, Simplaceanu V, Gong Q, et al. (2007). "Insights into the solution structure of human deoxyhemoglobin in the absence and presence of an allosteric effector". Biochemistry. 46 (35): 9973–80. doi:10.1021/bi700935z. PMC 2532491. PMID 17691822.
  • Sorour Y, Heppinstall S, Porter N, et al. (2007). "Is routine molecular screening for common alpha-thalassaemia deletions necessary as part of an antenatal screening programme?". Journal of Medical Screening. 14 (2): 60–1. doi:10.1258/096914107781261981. PMID 17626702. S2CID 24823660.
  • Hung CC, Lee CN, Chen CP, et al. (2007). "Molecular assay of -alpha(3.7) and -alpha(4.2) deletions causing alpha-thalassemia by denaturing high-performance liquid chromatography". Clin. Biochem. 40 (11): 817–21. doi:10.1016/j.clinbiochem.2007.03.018. PMID 17512924.
  • Ye BC, Zhang Z, Lei Z (2007). "Molecular analysis of alpha/beta-thalassemia in a southern Chinese population". Genet. Test. 11 (1): 75–83. doi:10.1089/gte.2006.0502. PMID 17394396.
  • Dilley J, Ganesan A, Deepa R, et al. (2007). "Association of A1C with cardiovascular disease and metabolic syndrome in Asian Indians with normal glucose tolerance". Diabetes Care. 30 (6): 1527–32. doi:10.2337/dc06-2414. PMID 17351274.
  • Fonseka PV, Vasudevan G, Clarizia LJ, McDonald MJ (2007). "Temperature dependent soret spectral band shifts accompany human CN-mesohemoglobin assembly". Protein J. 26 (4): 257–63. doi:10.1007/s10930-006-9067-7. PMID 17191128. S2CID 24601675.
  • Sankar VH, Arya V, Tewari D, et al. (2007). "Genotyping of alpha-thalassemia in microcytic hypochromic anemia patients from North India". J. Appl. Genet. 47 (4): 391–5. doi:10.1007/BF03194650. PMID 17132905. S2CID 19194610.
  • Origa R, Sollaino MC, Giagu N, et al. (2007). "Clinical and molecular analysis of haemoglobin H disease in Sardinia: haematological, obstetric and cardiac aspects in patients with different genotypes". Br. J. Haematol. 136 (2): 326–32. doi:10.1111/j.1365-2141.2006.06423.x. PMID 17129226. S2CID 23265827.
  • Hussein OA, Gefen Y, Zidan JM, et al. (2007). "LDL oxidation is associated with increased blood hemoglobin A1c levels in diabetic patients". Clin. Chim. Acta. 377 (1–2): 114–8. doi:10.1016/j.cca.2006.09.002. PMID 17070510.
  • Pan W, Galkin O, Filobelo L, et al. (2007). "Metastable mesoscopic clusters in solutions of sickle-cell hemoglobin". Biophys. J. 92 (1): 267–77. Bibcode:2007BpJ....92..267P. doi:10.1529/biophysj.106.094854. PMC 1697867. PMID 17040989.
  • Pistrosch F, Koehler C, Wildbrett J, Hanefeld M (2006). "Relationship between diurnal glucose levels and HbA1c in type 2 diabetes". Horm. Metab. Res. 38 (7): 455–9. doi:10.1055/s-2006-947838. PMID 16933182. S2CID 260166156.
  • Chong YM, Tan JA, Zubaidah Z, et al. (2006). "Screening of concurrent alpha-thalassaemia 1 in beta-thalassaemia carriers". Med. J. Malaysia. 61 (2): 217–20. PMID 16898315.

External links

  • GeneReviews/NCBI/NIH/UW entry on Alpha-Thalassemia
  • OMIM entries on Alpha-Thalassemia
  • Overview of all the structural information available in the PDB for UniProt: P69905 (Hemoglobin subunit alpha) at the PDBe-KB.
  • v
  • t
  • e
  • 1a00: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 TYR) MUTANT
    1a00: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 TYR) MUTANT
  • 1a01: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 ALA) MUTANT
    1a01: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 ALA) MUTANT
  • 1a0u: HEMOGLOBIN (VAL BETA1 MET) MUTANT
    1a0u: HEMOGLOBIN (VAL BETA1 MET) MUTANT
  • 1a0z: HEMOGLOBIN (VAL BETA1 MET) MUTANT
    1a0z: HEMOGLOBIN (VAL BETA1 MET) MUTANT
  • 1a3n: DEOXY HUMAN HEMOGLOBIN
    1a3n: DEOXY HUMAN HEMOGLOBIN
  • 1a3o: ARTIFICIAL MUTANT (ALPHA Y42H) OF DEOXY HEMOGLOBIN
    1a3o: ARTIFICIAL MUTANT (ALPHA Y42H) OF DEOXY HEMOGLOBIN
  • 1a9w: HUMAN EMBRYONIC GOWER II CARBONMONOXY HEMOGLOBIN
    1a9w: HUMAN EMBRYONIC GOWER II CARBONMONOXY HEMOGLOBIN
  • 1abw: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)
    1abw: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)
  • 1aby: CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)
    1aby: CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)
  • 1aj9: R-STATE HUMAN CARBONMONOXYHEMOGLOBIN ALPHA-A53S
    1aj9: R-STATE HUMAN CARBONMONOXYHEMOGLOBIN ALPHA-A53S
  • 1b86: HUMAN DEOXYHAEMOGLOBIN-2,3-DIPHOSPHOGLYCERATE COMPLEX
    1b86: HUMAN DEOXYHAEMOGLOBIN-2,3-DIPHOSPHOGLYCERATE COMPLEX
  • 1bab: HEMOGLOBIN THIONVILLE: AN ALPHA-CHAIN VARIANT WITH A SUBSTITUTION OF A GLUTAMATE FOR VALINE AT NA-1 AND HAVING AN ACETYLATED METHIONINE NH2 TERMINUS
    1bab: HEMOGLOBIN THIONVILLE: AN ALPHA-CHAIN VARIANT WITH A SUBSTITUTION OF A GLUTAMATE FOR VALINE AT NA-1 AND HAVING AN ACETYLATED METHIONINE NH2 TERMINUS
  • 1bbb: A THIRD QUATERNARY STRUCTURE OF HUMAN HEMOGLOBIN A AT 1.7-ANGSTROMS RESOLUTION
    1bbb: A THIRD QUATERNARY STRUCTURE OF HUMAN HEMOGLOBIN A AT 1.7-ANGSTROMS RESOLUTION
  • 1bij: CROSSLINKED, DEOXY HUMAN HEMOGLOBIN A
    1bij: CROSSLINKED, DEOXY HUMAN HEMOGLOBIN A
  • 1buw: CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A
    1buw: CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A
  • 1bz0: HEMOGLOBIN A (HUMAN, DEOXY, HIGH SALT)
    1bz0: HEMOGLOBIN A (HUMAN, DEOXY, HIGH SALT)
  • 1bz1: HEMOGLOBIN (ALPHA + MET) VARIANT
    1bz1: HEMOGLOBIN (ALPHA + MET) VARIANT
  • 1bzz: HEMOGLOBIN (ALPHA V1M) MUTANT
    1bzz: HEMOGLOBIN (ALPHA V1M) MUTANT
  • 1c7b: DEOXY RHB1.0 (RECOMBINANT HEMOGLOBIN)
    1c7b: DEOXY RHB1.0 (RECOMBINANT HEMOGLOBIN)
  • 1c7c: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)
    1c7c: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)
  • 1c7d: DEOXY RHB1.2 (RECOMBINANT HEMOGLOBIN)
    1c7d: DEOXY RHB1.2 (RECOMBINANT HEMOGLOBIN)
  • 1cls: CROSS-LINKED HUMAN HEMOGLOBIN DEOXY
    1cls: CROSS-LINKED HUMAN HEMOGLOBIN DEOXY
  • 1cmy: THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN
    1cmy: THE MUTATION BETA99 ASP-TYR STABILIZES Y-A NEW, COMPOSITE QUATERNARY STATE OF HUMAN HEMOGLOBIN
  • 1coh: STRUCTURE OF HAEMOGLOBIN IN THE DEOXY QUATERNARY STATE WITH LIGAND BOUND AT THE ALPHA HAEMS
    1coh: STRUCTURE OF HAEMOGLOBIN IN THE DEOXY QUATERNARY STATE WITH LIGAND BOUND AT THE ALPHA HAEMS
  • 1dke: NI BETA HEME HUMAN HEMOGLOBIN
    1dke: NI BETA HEME HUMAN HEMOGLOBIN
  • 1dxt: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI
    1dxt: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI
  • 1dxu: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI
    1dxu: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI
  • 1dxv: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI
    1dxv: HIGH-RESOLUTION X-RAY STUDY OF DEOXY RECOMBINANT HUMAN HEMOGLOBINS SYNTHESIZED FROM BETA-GLOBINS HAVING MUTATED AMINO TERMINI
  • 1fdh: STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN
    1fdh: STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN
  • 1fn3: CRYSTAL STRUCTURE OF NICKEL RECONSTITUTED HEMOGLOBIN-A CASE FOR PERMANENT, T-STATE HEMOGLOBIN
    1fn3: CRYSTAL STRUCTURE OF NICKEL RECONSTITUTED HEMOGLOBIN-A CASE FOR PERMANENT, T-STATE HEMOGLOBIN
  • 1g9v: HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXY HEMOGLOBIN COMPLEXED WITH A POTENT ALLOSTERIC EFFECTOR
    1g9v: HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXY HEMOGLOBIN COMPLEXED WITH A POTENT ALLOSTERIC EFFECTOR
  • 1gbu: DEOXY (BETA-(C93A,C112G)) HUMAN HEMOGLOBIN
    1gbu: DEOXY (BETA-(C93A,C112G)) HUMAN HEMOGLOBIN
  • 1gbv: (ALPHA-OXY, BETA-(C112G)DEOXY) T-STATE HUMAN HEMOGLOBIN
    1gbv: (ALPHA-OXY, BETA-(C112G)DEOXY) T-STATE HUMAN HEMOGLOBIN
  • 1gli: DEOXYHEMOGLOBIN T38W (ALPHA CHAINS), V1G (ALPHA AND BETA CHAINS)
    1gli: DEOXYHEMOGLOBIN T38W (ALPHA CHAINS), V1G (ALPHA AND BETA CHAINS)
  • 1gzx: OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS
    1gzx: OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS
  • 1hab: CROSSLINKED HAEMOGLOBIN
    1hab: CROSSLINKED HAEMOGLOBIN
  • 1hac: CROSSLINKED HAEMOGLOBIN
    1hac: CROSSLINKED HAEMOGLOBIN
  • 1hba: HIGH-RESOLUTION X-RAY STUDY OF DEOXYHEMOGLOBIN ROTHSCHILD 37BETA TRP-> ARG: A MUTATION THAT CREATES AN INTERSUBUNIT CHLORIDE-BINDING SITE
    1hba: HIGH-RESOLUTION X-RAY STUDY OF DEOXYHEMOGLOBIN ROTHSCHILD 37BETA TRP-> ARG: A MUTATION THAT CREATES AN INTERSUBUNIT CHLORIDE-BINDING SITE
  • 1hbb: HIGH-RESOLUTION X-RAY STUDY OF DEOXYHEMOGLOBIN ROTHSCHILD 37BETA TRP-> ARG: A MUTATION THAT CREATES AN INTERSUBUNIT CHLORIDE-BINDING SITE
    1hbb: HIGH-RESOLUTION X-RAY STUDY OF DEOXYHEMOGLOBIN ROTHSCHILD 37BETA TRP-> ARG: A MUTATION THAT CREATES AN INTERSUBUNIT CHLORIDE-BINDING SITE
  • 1hbs: REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION
    1hbs: REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION
  • 1hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION
    1hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION
  • 1hdb: ANALYSIS OF THE CRYSTAL STRUCTURE, MOLECULAR MODELING AND INFRARED SPECTROSCOPY OF THE DISTAL BETA-HEME POCKET VALINE67(E11)-THREONINE MUTATION OF HEMOGLOBIN
    1hdb: ANALYSIS OF THE CRYSTAL STRUCTURE, MOLECULAR MODELING AND INFRARED SPECTROSCOPY OF THE DISTAL BETA-HEME POCKET VALINE67(E11)-THREONINE MUTATION OF HEMOGLOBIN
  • 1hga: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
    1hga: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
  • 1hgb: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
    1hgb: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
  • 1hgc: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
    1hgc: HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
  • 1hho: STRUCTURE OF HUMAN OXYHAEMOGLOBIN AT 2.1 ANGSTROMS RESOLUTION
    1hho: STRUCTURE OF HUMAN OXYHAEMOGLOBIN AT 2.1 ANGSTROMS RESOLUTION
  • 1ird: Crystal Structure of Human Carbonmonoxy-Haemoglobin at 1.25 A Resolution
    1ird: Crystal Structure of Human Carbonmonoxy-Haemoglobin at 1.25 A Resolution
  • 1j3y: Direct observation of photolysis-induced tertiary structural changes in human hemoglobin; Crystal structure of alpha(Fe)-beta(Ni) hemoglobin (laser photolysed)
    1j3y: Direct observation of photolysis-induced tertiary structural changes in human hemoglobin; Crystal structure of alpha(Fe)-beta(Ni) hemoglobin (laser photolysed)
  • 1j3z: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Fe-CO)-beta(Ni) hemoglobin (laser unphotolysed)
    1j3z: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Fe-CO)-beta(Ni) hemoglobin (laser unphotolysed)
  • 1j40: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Ni)-beta(Fe-CO) hemoglobin (laser unphotolysed)
    1j40: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Ni)-beta(Fe-CO) hemoglobin (laser unphotolysed)
  • 1j41: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Ni)-beta(Fe) hemoglobin (laser photolysed)
    1j41: Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Ni)-beta(Fe) hemoglobin (laser photolysed)
  • 1j7s: Crystal Structure of deoxy HbalphaYQ, a mutant of HbA
    1j7s: Crystal Structure of deoxy HbalphaYQ, a mutant of HbA
  • 1j7w: Crystal structure of deoxy HbbetaYQ, a site directed mutant of HbA
    1j7w: Crystal structure of deoxy HbbetaYQ, a site directed mutant of HbA
  • 1j7y: Crystal structure of partially ligated mutant of HbA
    1j7y: Crystal structure of partially ligated mutant of HbA
  • 1jy7: THE STRUCTURE OF HUMAN METHEMOGLOBIN. THE VARIATION OF A THEME
    1jy7: THE STRUCTURE OF HUMAN METHEMOGLOBIN. THE VARIATION OF A THEME
  • 1k0y: X-ray Crystallographic Analyses of Symmetrical Allosteric Effectors of Hemoglobin. Compounds Designed to Link Primary and Secondary Binding Sites
    1k0y: X-ray Crystallographic Analyses of Symmetrical Allosteric Effectors of Hemoglobin. Compounds Designed to Link Primary and Secondary Binding Sites
  • 1k1k: Structure of Mutant Human Carbonmonoxyhemoglobin C (beta E6K) at 2.0 Angstrom Resolution in Phosphate Buffer.
    1k1k: Structure of Mutant Human Carbonmonoxyhemoglobin C (beta E6K) at 2.0 Angstrom Resolution in Phosphate Buffer.
  • 1kd2: Crystal Structure of Human Deoxyhemoglobin in Absence of Any Anions
    1kd2: Crystal Structure of Human Deoxyhemoglobin in Absence of Any Anions
  • 1lfl: DEOXY HEMOGLOBIN (90% RELATIVE HUMIDITY)
    1lfl: DEOXY HEMOGLOBIN (90% RELATIVE HUMIDITY)
  • 1lfq: OXY HEMOGLOBIN (93% RELATIVE HUMIDITY)
    1lfq: OXY HEMOGLOBIN (93% RELATIVE HUMIDITY)
  • 1lft: OXY HEMOGLOBIN (90% RELATIVE HUMIDITY)
    1lft: OXY HEMOGLOBIN (90% RELATIVE HUMIDITY)
  • 1lfv: OXY HEMOGLOBIN (88% RELATIVE HUMIDITY)
    1lfv: OXY HEMOGLOBIN (88% RELATIVE HUMIDITY)
  • 1lfy: OXY HEMOGLOBIN (84% RELATIVE HUMIDITY)
    1lfy: OXY HEMOGLOBIN (84% RELATIVE HUMIDITY)
  • 1lfz: OXY HEMOGLOBIN (25% METHANOL)
    1lfz: OXY HEMOGLOBIN (25% METHANOL)
  • 1ljw: Crystal Structure of Human Carbonmonoxy Hemoglobin at 2.16 A: A Snapshot of the Allosteric Transition
    1ljw: Crystal Structure of Human Carbonmonoxy Hemoglobin at 2.16 A: A Snapshot of the Allosteric Transition
  • 1m9p: Crystalline Human Carbonmonoxy Hemoglobin C Exhibits The R2 Quaternary State at Neutral pH In The Presence of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure
    1m9p: Crystalline Human Carbonmonoxy Hemoglobin C Exhibits The R2 Quaternary State at Neutral pH In The Presence of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure
  • 1mko: A Fourth Quaternary Structure of Human Hemoglobin A at 2.18 A Resolution
    1mko: A Fourth Quaternary Structure of Human Hemoglobin A at 2.18 A Resolution
  • 1nej: Crystalline Human Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Exhibits The R2 Quaternary State At Neutral pH In The Presence Of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure
    1nej: Crystalline Human Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Exhibits The R2 Quaternary State At Neutral pH In The Presence Of Polyethylene Glycol: The 2.1 Angstrom Resolution Crystal Structure
  • 1nih: Structure of deoxy-quaternary haemoglobin with liganded beta subunits
    1nih: Structure of deoxy-quaternary haemoglobin with liganded beta subunits
  • 1nqp: Crystal structure of Human hemoglobin E at 1.73 A resolution
    1nqp: Crystal structure of Human hemoglobin E at 1.73 A resolution
  • 1o1i: Cyanomet hemoglobin (A-GLY-C:V1M,L29F,H58Q; B,D:V1M,L106W)
    1o1i: Cyanomet hemoglobin (A-GLY-C:V1M,L29F,H58Q; B,D:V1M,L106W)
  • 1o1j: Deoxy hemoglobin (A-GLY-C:V1M,L29F,H58Q; B,D:V1M,L106W)
    1o1j: Deoxy hemoglobin (A-GLY-C:V1M,L29F,H58Q; B,D:V1M,L106W)
  • 1o1k: Deoxy hemoglobin (A,C:V1M; B,D:V1M,V67W)
    1o1k: Deoxy hemoglobin (A,C:V1M; B,D:V1M,V67W)
  • 1o1l: Deoxy hemoglobin (A-GLY-C:V1M,L29W,H58Q; B,D:V1M)
    1o1l: Deoxy hemoglobin (A-GLY-C:V1M,L29W,H58Q; B,D:V1M)
  • 1o1m: Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29F,H58Q B,D:V1M,V67W)
    1o1m: Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29F,H58Q B,D:V1M,V67W)
  • 1o1n: Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29W; B,D:V1M)
    1o1n: Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29W; B,D:V1M)
  • 1o1o: Deoxy hemoglobin (A,C:V1M,V62L; B,D:V1M,V67L)
    1o1o: Deoxy hemoglobin (A,C:V1M,V62L; B,D:V1M,V67L)
  • 1o1p: Deoxy hemoglobin (A-GLY-C:V1M; B,D:V1M,C93A,N108K)
    1o1p: Deoxy hemoglobin (A-GLY-C:V1M; B,D:V1M,C93A,N108K)
  • 1qi8: DEOXYGENATED STRUCTURE OF A DISTAL POCKET HEMOGLOBIN MUTANT
    1qi8: DEOXYGENATED STRUCTURE OF A DISTAL POCKET HEMOGLOBIN MUTANT
  • 1qsh: MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME
    1qsh: MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME
  • 1qsi: MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME
    1qsi: MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME
  • 1qxd: Structural Basis for the Potent Antisickling Effect of a Novel Class of 5-Membered Heterocyclic Aldehydic Compounds
    1qxd: Structural Basis for the Potent Antisickling Effect of a Novel Class of 5-Membered Heterocyclic Aldehydic Compounds
  • 1qxe: Structural Basis for the Potent Antisickling Effect of a Novel Class of 5-Membered Heterocyclic Aldehydic Compounds
    1qxe: Structural Basis for the Potent Antisickling Effect of a Novel Class of 5-Membered Heterocyclic Aldehydic Compounds
  • 1r1x: Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom
    1r1x: Crystal structure of oxy-human hemoglobin Bassett at 2.15 angstrom
  • 1r1y: Crystal structure of deoxy-human hemoglobin Bassett at 1.8 angstrom
    1r1y: Crystal structure of deoxy-human hemoglobin Bassett at 1.8 angstrom
  • 1rps: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin exposed to NO under anerobic conditions
    1rps: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Hemoglobin exposed to NO under anerobic conditions
  • 1rq3: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Deoxyhemoglobin, Deoxyhemoglobin
    1rq3: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Deoxyhemoglobin, Deoxyhemoglobin
  • 1rq4: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin, HEMOGLOBIN EXPOSED TO NO UNDER AEROBIC CONDITIONS
    1rq4: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin, HEMOGLOBIN EXPOSED TO NO UNDER AEROBIC CONDITIONS
  • 1rqa: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E hemoglobin exposed to NO under anaerobic conditions
    1rqa: Crystallographic Analysis of the Interaction of Nitric Oxide with Quaternary-T Human Hemoglobin. Beta W73E hemoglobin exposed to NO under anaerobic conditions
  • 1rvw: R STATE HUMAN HEMOGLOBIN [ALPHA V96W], CARBONMONOXY
    1rvw: R STATE HUMAN HEMOGLOBIN [ALPHA V96W], CARBONMONOXY
  • 1sdk: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A
    1sdk: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A
  • 1sdl: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A
    1sdl: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A
  • 1shr: Crystal structure of ferrocyanide bound human hemoglobin A2 at 1.88A resolution
    1shr: Crystal structure of ferrocyanide bound human hemoglobin A2 at 1.88A resolution
  • 1si4: Crystal structure of Human hemoglobin A2 (in R2 state) at 2.2 A resolution
    1si4: Crystal structure of Human hemoglobin A2 (in R2 state) at 2.2 A resolution
  • 1thb: REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION
    1thb: REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION
  • 1uiw: Crystal Structures of Unliganded and Half-Liganded Human Hemoglobin Derivatives Cross-Linked between Lys 82beta1 and Lys 82beta2
    1uiw: Crystal Structures of Unliganded and Half-Liganded Human Hemoglobin Derivatives Cross-Linked between Lys 82beta1 and Lys 82beta2
  • 1vwt: T STATE HUMAN HEMOGLOBIN [ALPHA V96W], ALPHA AQUOMET, BETA DEOXY
    1vwt: T STATE HUMAN HEMOGLOBIN [ALPHA V96W], ALPHA AQUOMET, BETA DEOXY
  • 1xxt: The T-to-T High Transitions in Human Hemoglobin: wild-type deoxy Hb A (low salt, one test set)
    1xxt: The T-to-T High Transitions in Human Hemoglobin: wild-type deoxy Hb A (low salt, one test set)
  • 1xy0: T-to-THigh Transitions in Human Hemoglobin: alphaK40G deoxy low-salt
    1xy0: T-to-THigh Transitions in Human Hemoglobin: alphaK40G deoxy low-salt
  • 1xye: T-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low salt
    1xye: T-to-THigh Transitions in Human Hemoglobin: alpha Y42A deoxy low salt
  • 1xz2: wild-type hemoglobin deoxy no-salt
    1xz2: wild-type hemoglobin deoxy no-salt
  • 1xz4: Intersubunit Interactions Associated with Tyr42alpha Stabilize the Quaternary-T Tetramer but are not Major Quaternary Constraints in Deoxyhemoglobin: alphaY42A deoxyhemoglobin no-salt
    1xz4: Intersubunit Interactions Associated with Tyr42alpha Stabilize the Quaternary-T Tetramer but are not Major Quaternary Constraints in Deoxyhemoglobin: alphaY42A deoxyhemoglobin no-salt
  • 1xz5: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaL91A deoxy low-salt
    1xz5: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaL91A deoxy low-salt
  • 1xz7: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaR92A deoxy low-salt
    1xz7: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaR92A deoxy low-salt
  • 1xzu: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaD94G deoxy low-salt
    1xzu: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaD94G deoxy low-salt
  • 1xzv: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaP95A deoxy low-salt
    1xzv: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaP95A deoxy low-salt
  • 1y01: Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin
    1y01: Crystal structure of AHSP bound to Fe(II) alpha-hemoglobin
  • 1y09: T-to-T(High) Quaternary Transitions in Human Hemoglobin: alphaN97A deoxy low-salt
    1y09: T-to-T(High) Quaternary Transitions in Human Hemoglobin: alphaN97A deoxy low-salt
  • 1y0a: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaY140A deoxy low-salt
    1y0a: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaY140A deoxy low-salt
  • 1y0c: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaY140F deoxy low-salt
    1y0c: T-to-THigh Quaternary Transitions in Human Hemoglobin: alphaY140F deoxy low-salt
  • 1y0d: T-to-THigh Quaternary Transitions in Human Hemoglobin: desArg141alpha deoxy low-salt
    1y0d: T-to-THigh Quaternary Transitions in Human Hemoglobin: desArg141alpha deoxy low-salt
  • 1y0t: T-to-T(High) Quaternary Transitions in Human Hemoglobin: betaV1M deoxy low-salt (1 test set)
    1y0t: T-to-T(High) Quaternary Transitions in Human Hemoglobin: betaV1M deoxy low-salt (1 test set)
  • 1y0w: T-to-THigh quaternary Transitions in Human Hemoglobin: betaV1M deoxy low-salt (10 test sets)
    1y0w: T-to-THigh quaternary Transitions in Human Hemoglobin: betaV1M deoxy low-salt (10 test sets)
  • 1y22: T-To-T(High) quaternary transitions in human hemoglobin: betaV33A deoxy low-salt (1 test set)
    1y22: T-To-T(High) quaternary transitions in human hemoglobin: betaV33A deoxy low-salt (1 test set)
  • 1y2z: T-To-T(High) quaternary transitions in human hemoglobin: betaV34G deoxy low-salt (1 test set)
    1y2z: T-To-T(High) quaternary transitions in human hemoglobin: betaV34G deoxy low-salt (1 test set)
  • 1y31: T-To-T(High) quaternary transitions in human hemoglobin: betaY35A deoxy low-salt (1 test set)
    1y31: T-To-T(High) quaternary transitions in human hemoglobin: betaY35A deoxy low-salt (1 test set)
  • 1y35: T-To-T(High) quaternary transitions in human hemoglobin: betaY35F deoxy low-salt (1 test set)
    1y35: T-To-T(High) quaternary transitions in human hemoglobin: betaY35F deoxy low-salt (1 test set)
  • 1y45: T-To-T(high) quaternary transitions in human hemoglobin: betaP36A deoxy low-salt (10 test sets)
    1y45: T-To-T(high) quaternary transitions in human hemoglobin: betaP36A deoxy low-salt (10 test sets)
  • 1y46: T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y deoxy low-salt (10 test sets)
    1y46: T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y deoxy low-salt (10 test sets)
  • 1y4b: T-To-T(High) quaternary transitions in human hemoglobin: betaW37H deoxy low-salt (10 test sets)
    1y4b: T-To-T(High) quaternary transitions in human hemoglobin: betaW37H deoxy low-salt (10 test sets)
  • 1y4f: T-To-T(High) quaternary transitions in human hemoglobin: betaW37A deoxy low-salt (10 test sets)
    1y4f: T-To-T(High) quaternary transitions in human hemoglobin: betaW37A deoxy low-salt (10 test sets)
  • 1y4g: T-To-T(High) quaternary transitions in human hemoglobin: betaW37G deoxy low-salt (10 test sets)
    1y4g: T-To-T(High) quaternary transitions in human hemoglobin: betaW37G deoxy low-salt (10 test sets)
  • 1y4p: T-To-T(high) quaternary transitions in human hemoglobin: betaW37E deoxy low-salt (10 test sets)
    1y4p: T-To-T(high) quaternary transitions in human hemoglobin: betaW37E deoxy low-salt (10 test sets)
  • 1y4q: T-To-T(High) quaternary transitions in human hemoglobin: betaF42A deoxy low-salt (1 test set)
    1y4q: T-To-T(High) quaternary transitions in human hemoglobin: betaF42A deoxy low-salt (1 test set)
  • 1y4r: T-To-T(High) quaternary transitions in human hemoglobin: betaF45A deoxy low-salt (1 test set)
    1y4r: T-To-T(High) quaternary transitions in human hemoglobin: betaF45A deoxy low-salt (1 test set)
  • 1y4v: T-To-T(High) quaternary transitions in human hemoglobin: betaC93A deoxy low-salt (1 test set)
    1y4v: T-To-T(High) quaternary transitions in human hemoglobin: betaC93A deoxy low-salt (1 test set)
  • 1y5f: T-To-T(High) quaternary transitions in human hemoglobin: betaL96A deoxy low-salt (1 test set)
    1y5f: T-To-T(High) quaternary transitions in human hemoglobin: betaL96A deoxy low-salt (1 test set)
  • 1y5j: T-To-T(High) quaternary transitions in human hemoglobin: betaH97A deoxy low-salt (1 test set)
    1y5j: T-To-T(High) quaternary transitions in human hemoglobin: betaH97A deoxy low-salt (1 test set)
  • 1y5k: T-To-T(High) quaternary transitions in human hemoglobin: betaD99A deoxy low-salt (10 test sets)
    1y5k: T-To-T(High) quaternary transitions in human hemoglobin: betaD99A deoxy low-salt (10 test sets)
  • 1y7c: T-To-T(High) quaternary transitions in human hemoglobin: betaP100A deoxy low-salt (1 test set)
    1y7c: T-To-T(High) quaternary transitions in human hemoglobin: betaP100A deoxy low-salt (1 test set)
  • 1y7d: T-To-T(High) quaternary transitions in human hemoglobin: betaP100G deoxy low-salt (1 test set)
    1y7d: T-To-T(High) quaternary transitions in human hemoglobin: betaP100G deoxy low-salt (1 test set)
  • 1y7g: T-To-T(high) quaternary transitions in human hemoglobin: betaN102A deoxy low-salt (1 test set)
    1y7g: T-To-T(high) quaternary transitions in human hemoglobin: betaN102A deoxy low-salt (1 test set)
  • 1y7z: T-To-T(High) quaternary transitions in human hemoglobin: betaN108A deoxy low-salt (1 test set)
    1y7z: T-To-T(High) quaternary transitions in human hemoglobin: betaN108A deoxy low-salt (1 test set)
  • 1y83: T-To-T(High) quaternary transitions in human hemoglobin: betaY145G deoxy low-salt (1 test set)
    1y83: T-To-T(High) quaternary transitions in human hemoglobin: betaY145G deoxy low-salt (1 test set)
  • 1y85: T-To-T(High) quaternary transitions in human hemoglobin: desHIS146beta deoxy low-salt
    1y85: T-To-T(High) quaternary transitions in human hemoglobin: desHIS146beta deoxy low-salt
  • 1y8w: T-To-T(High) quaternary transitions in human hemoglobin: alphaR92A oxy (2mM IHP, 20% PEG) (10 test sets)
    1y8w: T-To-T(High) quaternary transitions in human hemoglobin: alphaR92A oxy (2mM IHP, 20% PEG) (10 test sets)
  • 1ydz: T-To-T(High) quaternary transitions in human hemoglobin: alphaY140F oxy (2MM IHP, 20% PEG) (1 test set)
    1ydz: T-To-T(High) quaternary transitions in human hemoglobin: alphaY140F oxy (2MM IHP, 20% PEG) (1 test set)
  • 1ye0: T-To-T(High) quaternary transitions in human hemoglobin: betaV33A oxy (2MM IHP, 20% PEG) (1 test set)
    1ye0: T-To-T(High) quaternary transitions in human hemoglobin: betaV33A oxy (2MM IHP, 20% PEG) (1 test set)
  • 1ye1: T-To-T(High) quaternary transitions in human hemoglobin: betaY35A oxy (2MM IHP, 20% PEG) (1 test set)
    1ye1: T-To-T(High) quaternary transitions in human hemoglobin: betaY35A oxy (2MM IHP, 20% PEG) (1 test set)
  • 1ye2: T-To-T(High) quaternary transitions in human hemoglobin: betaY35F oxy (2MM IHP, 20% PEG) (1 test set)
    1ye2: T-To-T(High) quaternary transitions in human hemoglobin: betaY35F oxy (2MM IHP, 20% PEG) (1 test set)
  • 1yen: T-To-T(High) quaternary transitions in human hemoglobin: betaP36A oxy (2MM IHP, 20% PEG) (10 test sets)
    1yen: T-To-T(High) quaternary transitions in human hemoglobin: betaP36A oxy (2MM IHP, 20% PEG) (10 test sets)
  • 1yeo: T-To-T(High) quaternary transitions in human hemoglobin: betaW37A OXY (10 test sets)
    1yeo: T-To-T(High) quaternary transitions in human hemoglobin: betaW37A OXY (10 test sets)
  • 1yeq: T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y OXY (10 test sets)
    1yeq: T-To-T(High) quaternary transitions in human hemoglobin: betaW37Y OXY (10 test sets)
  • 1yeu: T-To-T(High) quaternary transitions in human hemoglobin: betaW37G OXY (10 test sets)
    1yeu: T-To-T(High) quaternary transitions in human hemoglobin: betaW37G OXY (10 test sets)
  • 1yev: T-To-T(High) quaternary transitions in human hemoglobin: betaW37E OXY (10 test sets)
    1yev: T-To-T(High) quaternary transitions in human hemoglobin: betaW37E OXY (10 test sets)
  • 1yff: STRUCTURE OF HUMAN CARBONMONOXYHEMOGLOBIN C (BETA E6K): TWO QUATERNARY STATES (R2 and R3) IN ONE CRYSTAL
    1yff: STRUCTURE OF HUMAN CARBONMONOXYHEMOGLOBIN C (BETA E6K): TWO QUATERNARY STATES (R2 and R3) IN ONE CRYSTAL
  • 1yg5: T-To-T(High) quaternary transitions in human hemoglobin: betaW37H OXY (2MM IHP, 20% PEG) (10 test sets)
    1yg5: T-To-T(High) quaternary transitions in human hemoglobin: betaW37H OXY (2MM IHP, 20% PEG) (10 test sets)
  • 1ygd: T-To-T(High) quaternary transitions in human hemoglobin: betaW37E alpha zinc beta oxy (10 TEST SETS)
    1ygd: T-To-T(High) quaternary transitions in human hemoglobin: betaW37E alpha zinc beta oxy (10 TEST SETS)
  • 1ygf: T-to-T(high) quaternary transitions in human hemoglobin: betaH97A oxy (2MM IHP, 20% PEG) (1 test set)
    1ygf: T-to-T(high) quaternary transitions in human hemoglobin: betaH97A oxy (2MM IHP, 20% PEG) (1 test set)
  • 1yh9: T-to-T(High) quaternary transitions in human hemoglobin: HbA OXY (2MM IHP, 20% PEG) (10 test sets)
    1yh9: T-to-T(High) quaternary transitions in human hemoglobin: HbA OXY (2MM IHP, 20% PEG) (10 test sets)
  • 1yhe: T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (5.0MM IHP, 20% PEG) (10 test sets)
    1yhe: T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (5.0MM IHP, 20% PEG) (10 test sets)
  • 1yhr: T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (10.0MM IHP, 20% PEG) (10 test sets)
    1yhr: T-To-T(High) quaternary transitions in human hemoglobin: HbA OXY (10.0MM IHP, 20% PEG) (10 test sets)
  • 1yie: T-to-thigh quaternary transitions in human hemoglobin: betaW37A oxy (2.2MM IHP, 13% PEG) (1 test set)
    1yie: T-to-thigh quaternary transitions in human hemoglobin: betaW37A oxy (2.2MM IHP, 13% PEG) (1 test set)
  • 1yih: T-to-T(High) quaternary transitions in human hemoglobin: betaP100A oxy (2.2MM IHP, 20% PEG) (1 test set)
    1yih: T-to-T(High) quaternary transitions in human hemoglobin: betaP100A oxy (2.2MM IHP, 20% PEG) (1 test set)
  • 1yvq: The low salt (PEG) crystal structure of CO Hemoglobin E (betaE26K) approaching physiological pH (pH 7.5)
    1yvq: The low salt (PEG) crystal structure of CO Hemoglobin E (betaE26K) approaching physiological pH (pH 7.5)
  • 1yvt: The high salt (phosphate) crystal structure of CO Hemoglobin E (Glu26Lys) at physiological pH (pH 7.35)
    1yvt: The high salt (phosphate) crystal structure of CO Hemoglobin E (Glu26Lys) at physiological pH (pH 7.35)
  • 1yzi: A novel quaternary structure of human carbonmonoxy hemoglobin
    1yzi: A novel quaternary structure of human carbonmonoxy hemoglobin
  • 1z8u: Crystal structure of oxidized alpha hemoglobin bound to AHSP
    1z8u: Crystal structure of oxidized alpha hemoglobin bound to AHSP
  • 2d5z: Crystal structure of T-state human hemoglobin complexed with three L35 molecules
    2d5z: Crystal structure of T-state human hemoglobin complexed with three L35 molecules
  • 2d60: Crystal structure of deoxy human hemoglobin complexed with two L35 molecules
    2d60: Crystal structure of deoxy human hemoglobin complexed with two L35 molecules
  • 2dn1: 1.25A resolution crystal structure of human hemoglobin in the oxy form
    2dn1: 1.25A resolution crystal structure of human hemoglobin in the oxy form
  • 2dn2: 1.25A resolution crystal structure of human hemoglobin in the deoxy form
    2dn2: 1.25A resolution crystal structure of human hemoglobin in the deoxy form
  • 2dn3: 1.25A resolution crystal structure of human hemoglobin in the carbonmonoxy form
    2dn3: 1.25A resolution crystal structure of human hemoglobin in the carbonmonoxy form
  • 2h35: Solution structure of Human normal adult hemoglobin
    2h35: Solution structure of Human normal adult hemoglobin
  • 2hbc: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES
    2hbc: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES
  • 2hbd: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES
    2hbd: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES
  • 2hbe: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES
    2hbe: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES
  • 2hbf: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES
    2hbf: HIGH RESOLUTION X-RAY STRUCTURES OF MYOGLOBIN-AND HEMOGLOBIN-ALKYL ISOCYANIDE COMPLEXES
  • 2hbs: THE HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S
    2hbs: THE HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S
  • 2hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION
    2hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 ANGSTROMS RESOLUTION
  • 2hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION
    2hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION
  • 2hhd: OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN
    2hhd: OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA-CHAINS IN HUMAN AND BOVINE HEMOGLOBIN
  • 2hhe: OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA CHAINS IN HUMAN AND BOVINE HEMOGLOBIN
    2hhe: OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA CHAINS IN HUMAN AND BOVINE HEMOGLOBIN
  • 3hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION
    3hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION
  • 4hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION
    4hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION
  • 6hbw: Crystal structure of deoxy-human hemoglobin beta6 glu->trp
    6hbw: Crystal structure of deoxy-human hemoglobin beta6 glu->trp
  • v
  • t
  • e
Proteins that contain heme (hemoproteins)
Globins
Hemoglobin
Subunits
Alpha locus on 16:
Beta locus on 11:
Tetramers
stages of
development:
Embryonic
Fetal
Adult
pathology:
Compounds
Other human
Nonhuman
Other
human:
plant:
Other
see also disorders of globin and globulin proteins