4M4B
Human Hemoglobin Nitroethane Modified
Summary for 4M4B
Entry DOI | 10.2210/pdb4m4b/pdb |
Related | 4M4A |
Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total) |
Functional Keywords | r-state, human hemoglobin, nitroethane modified, oxygen transport |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 2 |
Total formula weight | 32424.69 |
Authors | Yi, J.,Thomas, L.M.,Richter-Addo, G.B. (deposition date: 2013-08-06, release date: 2014-07-16, Last modification date: 2023-09-20) |
Primary citation | Yi, J.,Ye, G.,Thomas, L.M.,Richter-Addo, G.B. Degradation of human hemoglobin by organic C-nitroso compounds. Chem.Commun.(Camb.), 49:11179-11181, 2013 Cited by PubMed Abstract: The crystal structure of the nitrosomethane adduct of human Hb shows N-binding of the MeNO ligands to heme Fe. The structure of the EtNO adduct reveals a surprising 4.9 Å heme slippage in the β subunit, and explains the ability of C-nitroso compounds to degrade Hb removing it from circulation. PubMed: 24149619DOI: 10.1039/c3cc46174b PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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