Hemoglobin subunit alpha
HBA1 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Aliases | HBA1, HBA-T3, HBH, hemoglobin subunit alpha 1, METHBA, ECYT7 | ||||||||||||||||||||||||||||||||||||||||||||||||||
External IDs | OMIM: 141800; MGI: 96015; HomoloGene: 469; GeneCards: HBA1; OMA:HBA1 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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
- ^ a b c GRCh38: Ensembl release 89: ENSG00000206172 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000069919 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "HBA1 gene: MedlinePlus Genetics".
- ^ a b c d "Entrez Gene: HBA1 hemoglobin, alpha 1".
- ^ 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.
- ^ 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.
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- 1a00: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 TYR) MUTANT
- 1a01: HEMOGLOBIN (VAL BETA1 MET, TRP BETA37 ALA) MUTANT
- 1a0u: HEMOGLOBIN (VAL BETA1 MET) MUTANT
- 1a0z: HEMOGLOBIN (VAL BETA1 MET) MUTANT
- 1a3n: DEOXY HUMAN HEMOGLOBIN
- 1a3o: ARTIFICIAL MUTANT (ALPHA Y42H) OF DEOXY HEMOGLOBIN
- 1a9w: HUMAN EMBRYONIC GOWER II CARBONMONOXY HEMOGLOBIN
- 1abw: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)
- 1aby: CYANOMET RHB1.1 (RECOMBINANT HEMOGLOBIN)
- 1aj9: R-STATE HUMAN CARBONMONOXYHEMOGLOBIN ALPHA-A53S
- 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
- 1bbb: A THIRD QUATERNARY STRUCTURE OF HUMAN HEMOGLOBIN A AT 1.7-ANGSTROMS RESOLUTION
- 1bij: CROSSLINKED, DEOXY HUMAN HEMOGLOBIN A
- 1buw: CRYSTAL STRUCTURE OF S-NITROSO-NITROSYL HUMAN HEMOGLOBIN A
- 1bz0: HEMOGLOBIN A (HUMAN, DEOXY, HIGH SALT)
- 1bz1: HEMOGLOBIN (ALPHA + MET) VARIANT
- 1bzz: HEMOGLOBIN (ALPHA V1M) MUTANT
- 1c7b: DEOXY RHB1.0 (RECOMBINANT HEMOGLOBIN)
- 1c7c: DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)
- 1c7d: DEOXY RHB1.2 (RECOMBINANT HEMOGLOBIN)
- 1cls: CROSS-LINKED HUMAN HEMOGLOBIN DEOXY
- 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
- 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
- 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
- 1fdh: STRUCTURE OF HUMAN FOETAL DEOXYHAEMOGLOBIN
- 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
- 1gbu: DEOXY (BETA-(C93A,C112G)) HUMAN HEMOGLOBIN
- 1gbv: (ALPHA-OXY, BETA-(C112G)DEOXY) T-STATE HUMAN HEMOGLOBIN
- 1gli: DEOXYHEMOGLOBIN T38W (ALPHA CHAINS), V1G (ALPHA AND BETA CHAINS)
- 1gzx: OXY T STATE HAEMOGLOBIN: OXYGEN BOUND AT ALL FOUR HAEMS
- 1hab: 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
- 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
- 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
- 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
- 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
- 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)
- 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)
- 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
- 1j7w: Crystal structure of deoxy HbbetaYQ, a site directed mutant of HbA
- 1j7y: Crystal structure of partially ligated mutant of HbA
- 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
- 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
- 1lfl: DEOXY HEMOGLOBIN (90% RELATIVE HUMIDITY)
- 1lfq: OXY HEMOGLOBIN (93% RELATIVE HUMIDITY)
- 1lft: OXY HEMOGLOBIN (90% RELATIVE HUMIDITY)
- 1lfv: OXY HEMOGLOBIN (88% RELATIVE HUMIDITY)
- 1lfy: OXY HEMOGLOBIN (84% RELATIVE HUMIDITY)
- 1lfz: OXY HEMOGLOBIN (25% METHANOL)
- 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
- 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
- 1nih: Structure of deoxy-quaternary haemoglobin with liganded beta subunits
- 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)
- 1o1j: Deoxy hemoglobin (A-GLY-C:V1M,L29F,H58Q; B,D:V1M,L106W)
- 1o1k: Deoxy hemoglobin (A,C:V1M; B,D:V1M,V67W)
- 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)
- 1o1n: Deoxy hemoglobin (A-GLYGLYGLY-C:V1M,L29W; B,D:V1M)
- 1o1o: Deoxy hemoglobin (A,C:V1M,V62L; B,D:V1M,V67L)
- 1o1p: Deoxy hemoglobin (A-GLY-C:V1M; B,D:V1M,C93A,N108K)
- 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
- 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
- 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
- 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
- 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
- 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
- 1sdk: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A
- 1sdl: CROSS-LINKED, CARBONMONOXY HEMOGLOBIN A
- 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
- 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
- 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)
- 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
- 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
- 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
- 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
- 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
- 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
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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)
- 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
- 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)
- 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)
- 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)
- 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)
- 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)
- 1yzi: A novel quaternary structure of human carbonmonoxy hemoglobin
- 1z8u: Crystal structure of oxidized alpha hemoglobin bound to AHSP
- 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
- 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
- 2dn3: 1.25A resolution crystal structure of human hemoglobin in the carbonmonoxy form
- 2h35: Solution structure of Human normal adult hemoglobin
- 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
- 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
- 2hbs: THE HIGH RESOLUTION CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S
- 2hco: THE STRUCTURE OF HUMAN CARBONMONOXY HAEMOGLOBIN AT 2.7 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
- 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
- 4hhb: THE CRYSTAL STRUCTURE OF HUMAN DEOXYHAEMOGLOBIN AT 1.74 ANGSTROMS RESOLUTION
- 6hbw: Crystal structure of deoxy-human hemoglobin beta6 glu->trp