1JA0
CYPOR-W677X
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
| A | 0004128 | molecular_function | cytochrome-b5 reductase activity, acting on NAD(P)H |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0006809 | biological_process | nitric oxide biosynthetic process |
| A | 0007584 | biological_process | response to nutrient |
| A | 0008047 | molecular_function | enzyme activator activity |
| A | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0009437 | biological_process | carnitine metabolic process |
| A | 0009725 | biological_process | response to hormone |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0019395 | biological_process | fatty acid oxidation |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0022900 | biological_process | electron transport chain |
| A | 0032332 | biological_process | positive regulation of chondrocyte differentiation |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0043602 | biological_process | nitrate catabolic process |
| A | 0045880 | biological_process | positive regulation of smoothened signaling pathway |
| A | 0046210 | biological_process | nitric oxide catabolic process |
| A | 0047726 | molecular_function | iron-cytochrome-c reductase activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0061913 | biological_process | positive regulation of growth plate cartilage chondrocyte proliferation |
| A | 0070988 | biological_process | demethylation |
| A | 0071371 | biological_process | cellular response to gonadotropin stimulus |
| A | 0071372 | biological_process | cellular response to follicle-stimulating hormone stimulus |
| A | 0071375 | biological_process | cellular response to peptide hormone stimulus |
| A | 0071548 | biological_process | response to dexamethasone |
| A | 0090031 | biological_process | positive regulation of steroid hormone biosynthetic process |
| A | 0090346 | biological_process | organofluorine metabolic process |
| B | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
| B | 0004128 | molecular_function | cytochrome-b5 reductase activity, acting on NAD(P)H |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005829 | cellular_component | cytosol |
| B | 0006809 | biological_process | nitric oxide biosynthetic process |
| B | 0007584 | biological_process | response to nutrient |
| B | 0008047 | molecular_function | enzyme activator activity |
| B | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0009437 | biological_process | carnitine metabolic process |
| B | 0009725 | biological_process | response to hormone |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0019395 | biological_process | fatty acid oxidation |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0022900 | biological_process | electron transport chain |
| B | 0032332 | biological_process | positive regulation of chondrocyte differentiation |
| B | 0043066 | biological_process | negative regulation of apoptotic process |
| B | 0043602 | biological_process | nitrate catabolic process |
| B | 0045880 | biological_process | positive regulation of smoothened signaling pathway |
| B | 0046210 | biological_process | nitric oxide catabolic process |
| B | 0047726 | molecular_function | iron-cytochrome-c reductase activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0061913 | biological_process | positive regulation of growth plate cartilage chondrocyte proliferation |
| B | 0070988 | biological_process | demethylation |
| B | 0071371 | biological_process | cellular response to gonadotropin stimulus |
| B | 0071372 | biological_process | cellular response to follicle-stimulating hormone stimulus |
| B | 0071375 | biological_process | cellular response to peptide hormone stimulus |
| B | 0071548 | biological_process | response to dexamethasone |
| B | 0090031 | biological_process | positive regulation of steroid hormone biosynthetic process |
| B | 0090346 | biological_process | organofluorine metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD A 750 |
| Chain | Residue |
| A | HIS319 |
| A | VAL476 |
| A | TYR478 |
| A | GLY488 |
| A | VAL489 |
| A | ALA490 |
| A | THR491 |
| A | ALA538 |
| A | NAP752 |
| A | HOH805 |
| A | HOH807 |
| A | ARG424 |
| A | HOH819 |
| A | HOH864 |
| A | HOH887 |
| A | HOH888 |
| A | ARG454 |
| A | TYR455 |
| A | TYR456 |
| A | SER457 |
| A | CYS472 |
| A | ALA473 |
| A | VAL474 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FAD B 850 |
| Chain | Residue |
| B | HIS319 |
| B | ARG424 |
| B | ARG454 |
| B | TYR455 |
| B | TYR456 |
| B | SER457 |
| B | CYS472 |
| B | ALA473 |
| B | VAL474 |
| B | TYR478 |
| B | GLY488 |
| B | VAL489 |
| B | ALA490 |
| B | THR491 |
| B | NAP852 |
| B | HOH855 |
| B | HOH875 |
| B | HOH970 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FMN A 751 |
| Chain | Residue |
| A | SER86 |
| A | GLN87 |
| A | THR88 |
| A | GLY89 |
| A | THR90 |
| A | ALA91 |
| A | ALA138 |
| A | THR139 |
| A | GLY141 |
| A | GLY143 |
| A | LEU173 |
| A | GLY174 |
| A | ASN175 |
| A | TYR178 |
| A | HIS180 |
| A | PHE181 |
| A | ASN182 |
| A | ASP208 |
| A | LEU212 |
| A | VAL676 |
| A | HOH890 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP A 752 |
| Chain | Residue |
| A | ARG298 |
| A | SER457 |
| A | PRO533 |
| A | GLY534 |
| A | THR535 |
| A | CYS566 |
| A | SER596 |
| A | ARG597 |
| A | LYS602 |
| A | TYR604 |
| A | GLN606 |
| A | CYS630 |
| A | GLY631 |
| A | ASP632 |
| A | ASN635 |
| A | MET636 |
| A | ASP639 |
| A | ASP675 |
| A | VAL676 |
| A | FAD750 |
| A | HOH757 |
| A | HOH889 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAP B 852 |
| Chain | Residue |
| B | MET636 |
| B | ASP639 |
| B | ASP675 |
| B | VAL676 |
| B | FAD850 |
| B | HOH864 |
| B | HOH949 |
| B | HOH950 |
| B | ARG298 |
| B | SER457 |
| B | GLY534 |
| B | THR535 |
| B | CYS566 |
| B | ARG567 |
| B | SER596 |
| B | ARG597 |
| B | LYS602 |
| B | TYR604 |
| B | GLN606 |
| B | CYS630 |
| B | GLY631 |
| B | ASP632 |
| B | ASN635 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 144 |
| Details | Domain: {"description":"Flavodoxin-like","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 43 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19171935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21345800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2013","submissionDatabase":"PDB data bank","title":"Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.","authors":["Sugishima M.","Sato H.","Higashimoto Y.","Harada J.","Wada K.","Fukuyama K.","Noguchi M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21345800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19171935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21345800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19171935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21345800","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2013","submissionDatabase":"PDB data bank","title":"Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.","authors":["Sugishima M.","Sato H.","Higashimoto Y.","Harada J.","Wada K.","Fukuyama K.","Noguchi M."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11371558","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19171935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2013","submissionDatabase":"PDB data bank","title":"Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase.","authors":["Sugishima M.","Sato H.","Higashimoto Y.","Harada J.","Wada K.","Fukuyama K.","Noguchi M."]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fnb |
| Chain | Residue | Details |
| A | ASP675 | |
| A | SER457 | |
| A | CYS630 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1fnb |
| Chain | Residue | Details |
| B | ASP675 | |
| B | SER457 | |
| B | CYS630 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fnb |
| Chain | Residue | Details |
| A | TYR456 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fnb |
| Chain | Residue | Details |
| B | TYR456 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 117 |
| Chain | Residue | Details |
| A | SER457 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser |
| A | CYS630 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction |
| A | ASP675 | hydrogen bond acceptor, modifies pKa |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 117 |
| Chain | Residue | Details |
| B | SER457 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser |
| B | CYS630 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction |
| B | ASP675 | hydrogen bond acceptor, modifies pKa |
