1QSI

MAGNESIUM(II)-AND ZINC(II)-PROTOPORPHYRIN IX'S STABILIZE THE LOWEST OXYGEN AFFINITY STATE OF HUMAN HEMOGLOBIN EVEN MORE STRONGLY THAN DEOXYHEME

Summary for 1QSI
DescriptorPROTEIN (HEMOGLOBIN ALPHA CHAIN), PROTEIN (HEMOGLOBIN BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
Functional Keywordshemoglobin; oxygen affinity; allosteric effect; metal substitution; trigger mechanism; alpha co liganded, oxygen storage-transport complex, oxygen storage/transport
Biological sourceHomo sapiens (human)
More
Total number of polymer chains4
Total formula weight64539.99
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: 2011-07-13)
Primary citationMinagawa, H.,Miyazaki, G.,Morimoto, H.,Nakagawa, A.,Park, S.Y.,Shibayama, N.,Yun, K.M.
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
PubMed: 10512707
DOI: 110.1006/jmbi.1999.3124
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation
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PDB entries from 2021-06-23