Summary for 3PEL
| Entry DOI | 10.2210/pdb3pel/pdb |
| Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | globin fold, oxygen/co2 transport, heme binding, red blood cells, oxygen transport |
| Biological source | Canis lupus familiaris (dogs) More |
| Total number of polymer chains | 2 |
| Total formula weight | 32493.64 |
| Authors | Bhatt, V.S.,Zaldivar-Lopez, S.,Harris, D.R.,Couto, C.G.,Wang, P.G.,Palmer, A.F. (deposition date: 2010-10-26, release date: 2010-11-03, Last modification date: 2023-09-06) |
| Primary citation | Bhatt, V.S.,Zaldivar-Lopez, S.,Harris, D.R.,Couto, C.G.,Wang, P.G.,Palmer, A.F. Structure of Greyhound hemoglobin: origin of high oxygen affinity. Acta Crystallogr.,Sect.D, 67:395-402, 2011 Cited by PubMed Abstract: This study presents the crystal structure of Greyhound hemoglobin (GrHb) determined to 1.9 Å resolution. GrHb was found to crystallize with an α₁β₁ dimer in the asymmetric unit and belongs to the R2 state. Oxygen-affinity measurements combined with the fact that GrHb crystallizes in the R2 state despite the high-salt conditions used for crystallization strongly indicate that GrHb can serve as a model high-oxygen-affinity hemoglobin (Hb) for higher mammals, especially humans. Structural analysis of GrHb and its comparison with the R2-state of human Hb revealed several regions that can potentially contribute to the high oxygen affinity of GrHb and serve to rationalize the additional stability of the R2-state of GrHb. A previously well studied hydrophobic cluster of bar-headed goose Hb near α119 was also incorporated in the comparison between GrHb and human Hb. Finally, a structural comparison with generic dog Hb and maned wolf Hb was conducted, revealing that in contrast to GrHb these structures belong to the R state of Hb and raising the intriguing possibility of an additional allosteric factor co-purifying with GrHb that can modulate its quaternary structure. PubMed: 21543841DOI: 10.1107/S0907444911006044 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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