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; PubMed: 10512707; DOI: 10.1006/jmbi.1999.3124

Experimental method

X-RAY DIFFRACTION (1.7 Å)