1JA1
CYPOR-Triple Mutant
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 | 0005654 | cellular_component | nucleoplasm |
| 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 | 0018393 | biological_process | internal peptidyl-lysine acetylation |
| 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 | 0060192 | biological_process | negative regulation of lipase activity |
| 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 | 0005654 | cellular_component | nucleoplasm |
| 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 | 0018393 | biological_process | internal peptidyl-lysine acetylation |
| 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 | 0060192 | biological_process | negative regulation of lipase activity |
| 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 | 33 |
| Details | BINDING SITE FOR RESIDUE FAD A 1750 |
| Chain | Residue |
| A | HIS319 |
| A | TYR478 |
| A | GLY488 |
| A | VAL489 |
| A | ALA490 |
| A | THR491 |
| A | ARG514 |
| A | ALA538 |
| A | TRP677 |
| A | NAP1752 |
| A | HOH1759 |
| A | ARG424 |
| A | HOH1767 |
| A | HOH1783 |
| A | HOH1790 |
| A | HOH1795 |
| A | HOH1796 |
| A | HOH1828 |
| A | HOH1840 |
| A | HOH1866 |
| A | HOH1932 |
| A | HOH2023 |
| A | ARG454 |
| A | HOH2127 |
| A | HOH2339 |
| A | HOH2353 |
| A | HOH2372 |
| A | TYR455 |
| A | TYR456 |
| A | ALA457 |
| A | CYS472 |
| A | ALA473 |
| A | VAL474 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD B 1850 |
| Chain | Residue |
| B | HIS319 |
| B | ARG424 |
| B | ARG454 |
| B | TYR455 |
| B | TYR456 |
| B | ALA457 |
| B | CYS472 |
| B | ALA473 |
| B | VAL474 |
| B | TYR478 |
| B | GLY488 |
| B | VAL489 |
| B | ALA490 |
| B | THR491 |
| B | ARG514 |
| B | ALA538 |
| B | TRP677 |
| B | NAP1852 |
| B | HOH1854 |
| B | HOH1859 |
| B | HOH1889 |
| B | HOH1906 |
| B | HOH1917 |
| B | HOH1927 |
| B | HOH1946 |
| B | HOH1961 |
| B | HOH1970 |
| B | HOH2074 |
| B | HOH2092 |
| B | HOH2265 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FMN A 1751 |
| Chain | Residue |
| A | SER86 |
| A | GLN87 |
| A | THR88 |
| A | GLY89 |
| A | THR90 |
| A | ALA91 |
| A | ALA138 |
| A | THR139 |
| A | TYR140 |
| A | GLY141 |
| A | GLY143 |
| A | LEU173 |
| A | GLY174 |
| A | ASN175 |
| A | TYR178 |
| A | HIS180 |
| A | PHE181 |
| A | ASN182 |
| A | ASP208 |
| A | LEU212 |
| A | HOH1934 |
| A | HOH1942 |
| A | HOH2138 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN B 1851 |
| Chain | Residue |
| B | TYR178 |
| B | HIS180 |
| B | PHE181 |
| B | ASN182 |
| B | ASP208 |
| B | LEU212 |
| B | HOH2117 |
| B | SER86 |
| B | GLN87 |
| B | THR88 |
| B | GLY89 |
| B | THR90 |
| B | ALA91 |
| B | ALA138 |
| B | THR139 |
| B | TYR140 |
| B | GLY141 |
| B | LEU173 |
| B | GLY174 |
| B | ASN175 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAP A 1752 |
| Chain | Residue |
| A | ARG298 |
| A | GLY534 |
| A | THR535 |
| A | CYS566 |
| A | ARG567 |
| A | SER596 |
| A | ARG597 |
| A | LYS602 |
| A | TYR604 |
| A | GLN606 |
| A | ASN635 |
| A | MET636 |
| A | ASP639 |
| A | SER678 |
| A | FAD1750 |
| A | HOH1753 |
| A | HOH1770 |
| A | HOH1772 |
| A | HOH1996 |
| A | HOH2054 |
| A | HOH2121 |
| site_id | AC6 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAP B 1852 |
| Chain | Residue |
| B | ARG298 |
| B | GLY534 |
| B | THR535 |
| B | CYS566 |
| B | ARG567 |
| B | SER596 |
| B | ARG597 |
| B | LYS602 |
| B | TYR604 |
| B | GLN606 |
| B | ASP632 |
| B | ARG634 |
| B | ASN635 |
| B | MET636 |
| B | ASP639 |
| B | TRP677 |
| B | SER678 |
| B | FAD1850 |
| B | HOH1857 |
| B | HOH1867 |
| B | HOH1878 |
| B | HOH1891 |
| B | HOH1991 |
| B | HOH2009 |
| B | HOH2102 |
| B | HOH2159 |
| B | HOH2181 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EPE B 1753 |
| Chain | Residue |
| A | PRO435 |
| B | HIS607 |
| B | ASN635 |
| B | ASP639 |
| B | HOH1940 |
| B | HOH1990 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 288 |
| 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 | 484 |
| Details | Domain: {"description":"FAD-binding FR-type","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 62 |
| 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_FI4 |
| 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":"21345800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9237990","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| 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_FI6 |
| 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_FI7 |
| 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 | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| A | TYR456 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndh |
| Chain | Residue | Details |
| B | TYR456 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 117 |
| Chain | Residue | Details |
| A | ALA457 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser |
| A | ALA630 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction |
| A | ASN675 | hydrogen bond acceptor, modifies pKa |
| A | TRP677 | steric role |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 117 |
| Chain | Residue | Details |
| B | ALA457 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser |
| B | ALA630 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction |
| B | ASN675 | hydrogen bond acceptor, modifies pKa |
| B | TRP677 | steric role |
