3QFR
Crystal Structure of Human NADPH-Cytochrome P450 Reductase (R457H Mutant)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0009725 | biological_process | response to hormone |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0022900 | biological_process | electron transport chain |
| A | 0032770 | biological_process | positive regulation of monooxygenase activity |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0090346 | biological_process | cellular organofluorine metabolic process |
| B | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005829 | cellular_component | cytosol |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0009725 | biological_process | response to hormone |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0022900 | biological_process | electron transport chain |
| B | 0032770 | biological_process | positive regulation of monooxygenase activity |
| B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0090346 | biological_process | cellular organofluorine metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FAD A 752 |
| Chain | Residue |
| A | HOH2 |
| A | VAL477 |
| A | VAL479 |
| A | TYR481 |
| A | GLY491 |
| A | VAL492 |
| A | ALA493 |
| A | THR494 |
| A | TRP679 |
| A | HOH682 |
| A | FMN751 |
| A | HIS322 |
| A | ARG427 |
| A | HIS457 |
| A | TYR458 |
| A | TYR459 |
| A | SER460 |
| A | CYS475 |
| A | ALA476 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FMN A 751 |
| Chain | Residue |
| A | HOH7 |
| A | SER89 |
| A | GLN90 |
| A | THR91 |
| A | GLY92 |
| A | THR93 |
| A | ALA94 |
| A | ALA141 |
| A | THR142 |
| A | TYR143 |
| A | GLY144 |
| A | GLY146 |
| A | LEU176 |
| A | GLY177 |
| A | ASN178 |
| A | TYR181 |
| A | HIS183 |
| A | PHE184 |
| A | ASN185 |
| A | ASP211 |
| A | LEU215 |
| A | FAD752 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NAP A 753 |
| Chain | Residue |
| 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 | HOH697 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 761 |
| Chain | Residue |
| A | ASP255 |
| A | ASN595 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FAD B 752 |
| Chain | Residue |
| B | HOH1 |
| B | HIS322 |
| B | ARG427 |
| B | HIS457 |
| B | TYR458 |
| B | TYR459 |
| B | SER460 |
| B | CYS475 |
| B | ALA476 |
| B | VAL477 |
| B | VAL479 |
| B | TYR481 |
| B | GLY491 |
| B | VAL492 |
| B | ALA493 |
| B | THR494 |
| B | THR538 |
| B | ALA541 |
| B | TRP679 |
| B | FMN751 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN B 751 |
| Chain | Residue |
| B | SER89 |
| B | GLN90 |
| B | THR91 |
| B | GLY92 |
| B | THR93 |
| B | ALA94 |
| B | ALA141 |
| B | THR142 |
| B | TYR143 |
| B | GLY144 |
| B | GLY146 |
| B | LEU176 |
| B | GLY177 |
| B | ASN178 |
| B | TYR181 |
| B | HIS183 |
| B | PHE184 |
| B | ASN185 |
| B | ASP211 |
| B | LEU215 |
| B | FAD752 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAP B 753 |
| Chain | Residue |
| B | ARG301 |
| B | PRO536 |
| B | GLY537 |
| B | THR538 |
| B | CYS569 |
| B | ARG570 |
| B | SER599 |
| B | ARG600 |
| B | LYS605 |
| B | TYR607 |
| B | GLN609 |
| B | ASN637 |
| B | MET638 |
| B | ASP641 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:10048323, ECO:0000269|PubMed:21808038 |
| Chain | Residue | Details |
| A | SER89 | |
| A | ALA141 | |
| A | LEU176 | |
| A | ASP211 | |
| B | SER89 | |
| B | ALA141 | |
| B | LEU176 | |
| B | ASP211 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:21808038 |
| Chain | Residue | Details |
| A | ARG301 | |
| B | ASP641 | |
| A | THR538 | |
| A | SER599 | |
| A | LYS605 | |
| A | ASP641 | |
| B | ARG301 | |
| B | THR538 | |
| B | SER599 | |
| B | LYS605 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:19483672, ECO:0000269|PubMed:21808038 |
| Chain | Residue | Details |
| A | ARG427 | |
| B | TYR481 | |
| B | GLY491 | |
| B | TRP679 | |
| A | HIS457 | |
| A | CYS475 | |
| A | TYR481 | |
| A | GLY491 | |
| A | TRP679 | |
| B | ARG427 | |
| B | HIS457 | |
| B | CYS475 |
