1BVY
COMPLEX OF THE HEME AND FMN-BINDING DOMAINS OF THE CYTOCHROME P450(BM-3)
Summary for 1BVY
| Entry DOI | 10.2210/pdb1bvy/pdb |
| Descriptor | PROTEIN (CYTOCHROME P450 BM-3), PROTOPORPHYRIN IX CONTAINING FE, 1,2-ETHANEDIOL, ... (6 entities in total) |
| Functional Keywords | fatty acid monooxygenase, hemoprotein, flavoprotein, electron transfer, oxidoreductase |
| Biological source | Bacillus megaterium More |
| Cellular location | Cytoplasm (By similarity): P14779 P14779 |
| Total number of polymer chains | 3 |
| Total formula weight | 127593.78 |
| Authors | Sevrioukova, I.F.,Li, H.,Zhang, H.,Peterson, J.A.,Poulos, T.L. (deposition date: 1998-09-21, release date: 1999-02-23, Last modification date: 2023-08-09) |
| Primary citation | Sevrioukova, I.F.,Li, H.,Zhang, H.,Peterson, J.A.,Poulos, T.L. Structure of a cytochrome P450-redox partner electron-transfer complex. Proc.Natl.Acad.Sci.USA, 96:1863-1868, 1999 Cited by PubMed Abstract: The crystal structure of the complex between the heme- and FMN-binding domains of bacterial cytochrome P450BM-3, a prototype for the complex between eukaryotic microsomal P450s and P450 reductase, has been determined at 2.03 A resolution. The flavodoxin-like flavin domain is positioned at the proximal face of the heme domain with the FMN 4.0 and 18.4 A from the peptide that precedes the heme-binding loop and the heme iron, respectively. The heme-binding peptide represents the most efficient and coupled through-bond electron pathway to the heme iron. Substantial differences between the FMN-binding domains of P450BM-3 and microsomal P450 reductase, observed around the flavin-binding sites, are responsible for different redox properties of the FMN, which, in turn, control electron flow to the P450. PubMed: 10051560DOI: 10.1073/pnas.96.5.1863 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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