3QFC
Crystal Structure of Human NADPH-Cytochrome P450 (V492E 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 | 32 |
Details | BINDING SITE FOR RESIDUE FAD A 752 |
Chain | Residue |
A | HOH1 |
A | TYR459 |
A | SER460 |
A | CYS475 |
A | ALA476 |
A | VAL477 |
A | VAL479 |
A | TYR481 |
A | GLY491 |
A | GLU492 |
A | ALA493 |
A | HOH3 |
A | THR494 |
A | TRP679 |
A | HOH721 |
A | HOH735 |
A | FMN751 |
A | HOH835 |
A | HOH866 |
A | HOH955 |
A | HOH988 |
A | HOH1059 |
A | HOH6 |
A | HOH1086 |
A | HOH1107 |
A | HOH1189 |
A | HOH33 |
A | HOH55 |
A | HIS322 |
A | ARG427 |
A | ARG457 |
A | TYR458 |
site_id | AC2 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE FMN A 751 |
Chain | Residue |
A | HOH31 |
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 | LEU215 |
A | HOH713 |
A | FAD752 |
A | HOH807 |
A | HOH933 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAP A 753 |
Chain | Residue |
A | HOH19 |
A | ARG301 |
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 | HOH683 |
A | HOH776 |
A | HOH980 |
A | HOH1109 |
A | HOH1124 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 762 |
Chain | Residue |
A | HOH34 |
A | ASN595 |
A | HOH710 |
A | HOH912 |
A | HOH990 |
A | HOH1190 |
A | HOH1191 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE FAD B 752 |
Chain | Residue |
B | HOH711 |
B | FMN751 |
B | HOH760 |
B | HOH776 |
B | HIS322 |
B | ARG427 |
B | ARG457 |
B | TYR458 |
B | TYR459 |
B | SER460 |
B | CYS475 |
B | ALA476 |
B | VAL477 |
B | VAL479 |
B | GLY491 |
B | GLU492 |
B | ALA493 |
B | THR494 |
B | ALA541 |
B | TRP679 |
B | HOH702 |
site_id | AC6 |
Number of Residues | 22 |
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 | HOH705 |
B | FAD752 |
site_id | AC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAP B 753 |
Chain | Residue |
B | ARG301 |
B | GLY537 |
B | THR538 |
B | CYS569 |
B | ARG570 |
B | SER599 |
B | ARG600 |
B | LYS605 |
B | TYR607 |
B | GLN609 |
B | ARG636 |
B | ASN637 |
B | MET638 |
B | ASP641 |
B | TRP679 |
B | SER680 |
B | HOH706 |
B | HOH721 |
B | HOH782 |
B | HOH800 |
B | HOH831 |
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 | ARG457 | |
A | CYS475 | |
A | TYR481 | |
A | GLY491 | |
A | TRP679 | |
B | ARG427 | |
B | ARG457 | |
B | CYS475 |