2E2Y
Crystal Structure of F43W/H64D/V68I Myoglobin
Summary for 2E2Y
| Entry DOI | 10.2210/pdb2e2y/pdb |
| Descriptor | Myoglobin, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| Functional Keywords | oxygen storage/transport, oxygen storage-transport complex |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18391.94 |
| Authors | Ohki, T.,Ueno, T.,Hikage, T.,Suzuki, A.,Yamane, T.,Watanabe, Y. (deposition date: 2006-11-18, release date: 2007-10-23, Last modification date: 2023-10-25) |
| Primary citation | Watanabe, Y.,Nakajima, H.,Ueno, T. Reactivities of oxo and peroxo intermediates studied by hemoprotein mutants Acc.Chem.Res., 40:554-562, 2007 Cited by PubMed Abstract: A series of myoglobin mutants, in which distal sites are modified by site-directed mutagenesis, are able to catalyze peroxidase, catalase, and P450 reactions even though their proximal histidine ligands are intact. More importantly, reactions of P450, catalase, and peroxidase substrates and compound I of myoglobin mutants can be observed spectroscopically. Thus, detailed oxidation mechanisms were examined. On the basis of these results, we suggest that the different reactivities of P450, catalase, and peroxidase are mainly caused by their active site structures, but not the axial ligand. We have also prepared compound 0 under physiological conditions by employing a mutant of cytochrome c 552. Compound 0 is not able to oxidize ascorbic acid. PubMed: 17567089DOI: 10.1021/ar600046a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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