1SMI
A single mutation of P450 BM3 induces the conformational rearrangement seen upon substrate-binding in wild-type enzyme
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | Bifunctional P-450:NADPH-P450 reductase | polymer | 471 | 53854.3 | 2 | UniProt (P14779) Pfam (PF00067) | Bacillus megaterium | Cytochrome P450(BM-3); P450BM-3 [Includes: Cytochrome P450 102, NADPH--cytochrome P450 reductase]; ;cytochrome P-450:NADPH-P-450 reductase |
| 2 | C, D (A, B) | PROTOPORPHYRIN IX CONTAINING FE | non-polymer | 616.5 | 2 | Chemie (HEM) | |||
| 3 | E, F (A, B) | water | water | 18.0 | 492 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 471 (UniProt: P14779)
| PDB | External Database | Details |
|---|---|---|
| Glu 264 | Ala 264 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 107708.7 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 1233.0 | |
| All* | Total formula weight | 108941.6 |
