1OXA
CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)
Summary for 1OXA
| Entry DOI | 10.2210/pdb1oxa/pdb |
| Descriptor | CYTOCHROME P450 ERYF, PROTOPORPHYRIN IX CONTAINING FE, 6-DEOXYERYTHRONOLIDE B, ... (4 entities in total) |
| Functional Keywords | oxidoreductase (oxygenase) |
| Biological source | Saccharopolyspora erythraea |
| Cellular location | Cytoplasm (By similarity): Q00441 |
| Total number of polymer chains | 1 |
| Total formula weight | 45518.16 |
| Authors | Cupp-Vickery, J.R.,Poulos, T.L. (deposition date: 1995-07-14, release date: 1995-12-07, Last modification date: 2024-02-14) |
| Primary citation | Cupp-Vickery, J.R.,Poulos, T.L. Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nat.Struct.Biol., 2:144-153, 1995 Cited by PubMed Abstract: Cytochrome P450eryF catalyzes the 6S-hydroxylation of 6-deoxyerythronolide B, the initial reaction in a multistep pathway to convert 6-deoxyerythronolide B into the antibiotic, erythromycin. The overall structure of P450eryF is similar to that of P450cam but differs in the exact positioning of several alpha-helices. The largest difference occurs in the B' helix and results in the enlargement of the substrate-binding pocket of P450eryF. The substrate is positioned with the macrolide ring perpendicular to the haem plane and contacts seven hydrophobic residues and three solvent molecules. The substrate participates in a network of hydrogen bonds that may provide a proton shuttle pathway in the oxygen cleavage reaction. PubMed: 7749919DOI: 10.1038/nsb0295-144 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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