2HHE
OXYGEN AFFINITY MODULATION BY THE N-TERMINI OF THE BETA CHAINS IN HUMAN AND BOVINE HEMOGLOBIN
Summary for 2HHE
Entry DOI | 10.2210/pdb2hhe/pdb |
Descriptor | HEMOGLOBIN (DEOXY) (ALPHA CHAIN), HEMOGLOBIN (DEOXY) (BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
Functional Keywords | oxygen transport |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 4 |
Total formula weight | 64334.89 |
Authors | Gilliland, G.L.,Pechik, I.,Fronticelli, C.,Ji, X. (deposition date: 1994-09-29, release date: 1995-01-26, Last modification date: 2023-08-30) |
Primary citation | Fronticelli, C.,Pechik, I.,Brinigar, W.S.,Kowalczyk, J.,Gilliland, G.L. Chloride ion independence of the Bohr effect in a mutant human hemoglobin beta (V1M+H2deleted). J.Biol.Chem., 269:23965-23969, 1994 Cited by PubMed: 7929044PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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