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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7L18

Crystal structure of a tandem deletion mutant of rat NADPH-cytochrome P450 reductase

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003958molecular_functionNADPH-hemoprotein reductase activity
AAA0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
AAA0005654cellular_componentnucleoplasm
AAA0005737cellular_componentcytoplasm
AAA0005789cellular_componentendoplasmic reticulum membrane
AAA0005829cellular_componentcytosol
AAA0006809biological_processnitric oxide biosynthetic process
AAA0007584biological_processresponse to nutrient
AAA0008047molecular_functionenzyme activator activity
AAA0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
AAA0009055molecular_functionelectron transfer activity
AAA0009410biological_processresponse to xenobiotic stimulus
AAA0009437biological_processcarnitine metabolic process
AAA0009725biological_processresponse to hormone
AAA0010181molecular_functionFMN binding
AAA0016491molecular_functionoxidoreductase activity
AAA0016787molecular_functionhydrolase activity
AAA0018393biological_processinternal peptidyl-lysine acetylation
AAA0019395biological_processfatty acid oxidation
AAA0019899molecular_functionenzyme binding
AAA0022900biological_processelectron transport chain
AAA0032332biological_processpositive regulation of chondrocyte differentiation
AAA0043066biological_processnegative regulation of apoptotic process
AAA0043602biological_processnitrate catabolic process
AAA0045880biological_processpositive regulation of smoothened signaling pathway
AAA0046210biological_processnitric oxide catabolic process
AAA0047726molecular_functioniron-cytochrome-c reductase activity
AAA0050660molecular_functionflavin adenine dinucleotide binding
AAA0050661molecular_functionNADP binding
AAA0060192biological_processnegative regulation of lipase activity
AAA0061913biological_processpositive regulation of growth plate cartilage chondrocyte proliferation
AAA0070988biological_processdemethylation
AAA0071371biological_processcellular response to gonadotropin stimulus
AAA0071372biological_processcellular response to follicle-stimulating hormone stimulus
AAA0071375biological_processcellular response to peptide hormone stimulus
AAA0071548biological_processresponse to dexamethasone
AAA0090031biological_processpositive regulation of steroid hormone biosynthetic process
AAA0090346biological_processorganofluorine metabolic process
BBB0003958molecular_functionNADPH-hemoprotein reductase activity
BBB0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
BBB0005654cellular_componentnucleoplasm
BBB0005737cellular_componentcytoplasm
BBB0005789cellular_componentendoplasmic reticulum membrane
BBB0005829cellular_componentcytosol
BBB0006809biological_processnitric oxide biosynthetic process
BBB0007584biological_processresponse to nutrient
BBB0008047molecular_functionenzyme activator activity
BBB0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
BBB0009055molecular_functionelectron transfer activity
BBB0009410biological_processresponse to xenobiotic stimulus
BBB0009437biological_processcarnitine metabolic process
BBB0009725biological_processresponse to hormone
BBB0010181molecular_functionFMN binding
BBB0016491molecular_functionoxidoreductase activity
BBB0016787molecular_functionhydrolase activity
BBB0018393biological_processinternal peptidyl-lysine acetylation
BBB0019395biological_processfatty acid oxidation
BBB0019899molecular_functionenzyme binding
BBB0022900biological_processelectron transport chain
BBB0032332biological_processpositive regulation of chondrocyte differentiation
BBB0043066biological_processnegative regulation of apoptotic process
BBB0043602biological_processnitrate catabolic process
BBB0045880biological_processpositive regulation of smoothened signaling pathway
BBB0046210biological_processnitric oxide catabolic process
BBB0047726molecular_functioniron-cytochrome-c reductase activity
BBB0050660molecular_functionflavin adenine dinucleotide binding
BBB0050661molecular_functionNADP binding
BBB0060192biological_processnegative regulation of lipase activity
BBB0061913biological_processpositive regulation of growth plate cartilage chondrocyte proliferation
BBB0070988biological_processdemethylation
BBB0071371biological_processcellular response to gonadotropin stimulus
BBB0071372biological_processcellular response to follicle-stimulating hormone stimulus
BBB0071375biological_processcellular response to peptide hormone stimulus
BBB0071548biological_processresponse to dexamethasone
BBB0090031biological_processpositive regulation of steroid hormone biosynthetic process
BBB0090346biological_processorganofluorine metabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues288
DetailsDomain: {"description":"Flavodoxin-like","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues62
DetailsBinding 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."]}}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsBinding 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"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsBinding 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"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsBinding 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."]}}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding 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."]}}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 117
ChainResidueDetails
site_idMCSA2
Number of Residues3
DetailsM-CSA 117
ChainResidueDetails

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