1QSH
MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME
Summary for 1QSH
Entry DOI | 10.2210/pdb1qsh/pdb |
Related | 1QSI |
Descriptor | PROTEIN (HEMOGLOBIN ALPHA CHAIN), PROTEIN (HEMOGLOBIN BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
Functional Keywords | hemoglobin; oxygen affinity; allosteric effect; metal substitution; trigger mechanism, oxygen storage-transport complex, oxygen storage/transport |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 4 |
Total formula weight | 64483.97 |
Authors | Miyazaki, G.,Morimoto, H.,Yun, K.-M.,Park, S.-Y.,Nakagawa, A.,Minagawa, H.,Shibayama, N. (deposition date: 1999-06-22, release date: 1999-07-02, Last modification date: 2024-02-14) |
Primary citation | Miyazaki, G.,Morimoto, H.,Yun, K.M.,Park, S.Y.,Nakagawa, A.,Minagawa, H.,Shibayama, N. Magnesium(II) and zinc(II)-protoporphyrin IX's stabilize the lowest oxygen affinity state of human hemoglobin even more strongly than deoxyheme. J.Mol.Biol., 292:1121-1136, 1999 Cited by PubMed: 10512707DOI: 10.1006/jmbi.1999.3124 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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