1HDA
A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. STRUCTURE OF BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF SPECIFIC CHLORIDE-BINDING SITES AND ORIGIN OF THE CHLORIDE-LINKED BOHR EFFECT IN BOVINE AND HUMAN HAEMOGLOBIN
Summary for 1HDA
Entry DOI | 10.2210/pdb1hda/pdb |
Descriptor | HEMOGLOBIN (DEOXY) (ALPHA CHAIN), HEMOGLOBIN (DEOXY) (BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
Functional Keywords | oxygen transport |
Biological source | Bos taurus (cattle) More |
Total number of polymer chains | 4 |
Total formula weight | 64575.05 |
Authors | Fermi, G. (deposition date: 1993-05-06, release date: 1994-05-31, Last modification date: 2024-02-07) |
Primary citation | Perutz, M.F.,Fermi, G.,Poyart, C.,Pagnier, J.,Kister, J. A novel allosteric mechanism in haemoglobin. Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. J.Mol.Biol., 233:536-545, 1993 Cited by PubMed: 8411160DOI: 10.1006/jmbi.1993.1530 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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