3QFT
Crystal Structure of NADPH-Cytochrome P450 Reductase (FAD/NADPH domain and R457H Mutant)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD A 752 |
| Chain | Residue |
| A | HOH1 |
| A | ARG427 |
| A | HIS457 |
| A | TYR458 |
| A | TYR459 |
| A | SER460 |
| A | CYS475 |
| A | ALA476 |
| A | VAL477 |
| A | VAL479 |
| A | TYR481 |
| A | HOH5 |
| A | GLY491 |
| A | VAL492 |
| A | ALA493 |
| A | THR494 |
| A | ARG517 |
| A | TRP679 |
| A | HOH14 |
| A | HOH23 |
| A | HOH27 |
| A | HOH31 |
| A | HOH81 |
| A | HOH91 |
| A | HIS322 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP A 753 |
| Chain | Residue |
| A | HOH6 |
| A | HOH19 |
| A | HOH70 |
| A | HOH156 |
| A | HOH194 |
| A | ARG301 |
| A | PRO536 |
| A | GLY537 |
| A | THR538 |
| A | CYS569 |
| A | ARG570 |
| A | SER599 |
| A | ARG600 |
| A | LYS605 |
| A | TYR607 |
| A | GLN609 |
| A | ASN637 |
| A | MET638 |
| A | ASP641 |
| A | HOH764 |
| A | HOH883 |
| A | HOH890 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21808038","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19483672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21808038","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
