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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3ES9

NADPH-Cytochrome P450 Reductase in an Open Conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0003958molecular_functionNADPH-hemoprotein reductase activity
A0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005789cellular_componentendoplasmic reticulum membrane
A0005829cellular_componentcytosol
A0006809biological_processnitric oxide biosynthetic process
A0007584biological_processresponse to nutrient
A0008047molecular_functionenzyme activator activity
A0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
A0009055molecular_functionelectron transfer activity
A0009410biological_processresponse to xenobiotic stimulus
A0009437biological_processcarnitine metabolic process
A0009725biological_processresponse to hormone
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0018393biological_processinternal peptidyl-lysine acetylation
A0019395biological_processfatty acid oxidation
A0019899molecular_functionenzyme binding
A0022900biological_processelectron transport chain
A0032332biological_processpositive regulation of chondrocyte differentiation
A0043066biological_processnegative regulation of apoptotic process
A0043602biological_processnitrate catabolic process
A0045880biological_processpositive regulation of smoothened signaling pathway
A0046210biological_processnitric oxide catabolic process
A0047726molecular_functioniron-cytochrome-c reductase activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0060192biological_processnegative regulation of lipase activity
A0061913biological_processpositive regulation of growth plate cartilage chondrocyte proliferation
A0070988biological_processdemethylation
A0071371biological_processcellular response to gonadotropin stimulus
A0071372biological_processcellular response to follicle-stimulating hormone stimulus
A0071375biological_processcellular response to peptide hormone stimulus
A0071548biological_processresponse to dexamethasone
A0090031biological_processpositive regulation of steroid hormone biosynthetic process
A0090346biological_processorganofluorine metabolic process
B0003958molecular_functionNADPH-hemoprotein reductase activity
B0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0006809biological_processnitric oxide biosynthetic process
B0007584biological_processresponse to nutrient
B0008047molecular_functionenzyme activator activity
B0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
B0009055molecular_functionelectron transfer activity
B0009410biological_processresponse to xenobiotic stimulus
B0009437biological_processcarnitine metabolic process
B0009725biological_processresponse to hormone
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016787molecular_functionhydrolase activity
B0018393biological_processinternal peptidyl-lysine acetylation
B0019395biological_processfatty acid oxidation
B0019899molecular_functionenzyme binding
B0022900biological_processelectron transport chain
B0032332biological_processpositive regulation of chondrocyte differentiation
B0043066biological_processnegative regulation of apoptotic process
B0043602biological_processnitrate catabolic process
B0045880biological_processpositive regulation of smoothened signaling pathway
B0046210biological_processnitric oxide catabolic process
B0047726molecular_functioniron-cytochrome-c reductase activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
B0060192biological_processnegative regulation of lipase activity
B0061913biological_processpositive regulation of growth plate cartilage chondrocyte proliferation
B0070988biological_processdemethylation
B0071371biological_processcellular response to gonadotropin stimulus
B0071372biological_processcellular response to follicle-stimulating hormone stimulus
B0071375biological_processcellular response to peptide hormone stimulus
B0071548biological_processresponse to dexamethasone
B0090031biological_processpositive regulation of steroid hormone biosynthetic process
B0090346biological_processorganofluorine metabolic process
C0003958molecular_functionNADPH-hemoprotein reductase activity
C0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005789cellular_componentendoplasmic reticulum membrane
C0005829cellular_componentcytosol
C0006809biological_processnitric oxide biosynthetic process
C0007584biological_processresponse to nutrient
C0008047molecular_functionenzyme activator activity
C0008941molecular_functionnitric oxide dioxygenase NAD(P)H activity
C0009055molecular_functionelectron transfer activity
C0009410biological_processresponse to xenobiotic stimulus
C0009437biological_processcarnitine metabolic process
C0009725biological_processresponse to hormone
C0010181molecular_functionFMN binding
C0016491molecular_functionoxidoreductase activity
C0016787molecular_functionhydrolase activity
C0018393biological_processinternal peptidyl-lysine acetylation
C0019395biological_processfatty acid oxidation
C0019899molecular_functionenzyme binding
C0022900biological_processelectron transport chain
C0032332biological_processpositive regulation of chondrocyte differentiation
C0043066biological_processnegative regulation of apoptotic process
C0043602biological_processnitrate catabolic process
C0045880biological_processpositive regulation of smoothened signaling pathway
C0046210biological_processnitric oxide catabolic process
C0047726molecular_functioniron-cytochrome-c reductase activity
C0050660molecular_functionflavin adenine dinucleotide binding
C0050661molecular_functionNADP binding
C0060192biological_processnegative regulation of lipase activity
C0061913biological_processpositive regulation of growth plate cartilage chondrocyte proliferation
C0070988biological_processdemethylation
C0071371biological_processcellular response to gonadotropin stimulus
C0071372biological_processcellular response to follicle-stimulating hormone stimulus
C0071375biological_processcellular response to peptide hormone stimulus
C0071548biological_processresponse to dexamethasone
C0090031biological_processpositive regulation of steroid hormone biosynthetic process
C0090346biological_processorganofluorine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
ASER86
AGLY141
ALEU173
AGLY174
AASN175
ATYR178
AHIS180
APHE181
AASN182
AASP208
ALEU212
AGLN87
ATHR88
AGLY89
ATHR90
AALA91
AALA138
ATHR139
ATYR140
site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FAD A 752
ChainResidue
AHIS319
AARG424
AARG454
ATYR455
ATYR456
ASER457
ACYS472
AALA473
AVAL474
AVAL476
ATYR478
AGLY488
AVAL489
AALA490
ATHR491
ATRP677
site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE NAP A 753
ChainResidue
AARG298
AGLY534
ATHR535
ACYS566
AARG567
ASER596
AARG597
ALYS602
ATYR604
AGLN606
AARG634
AASN635
AASP639
site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE FAD B 752
ChainResidue
BARG424
BARG454
BTYR455
BTYR456
BSER457
BCYS472
BALA473
BVAL474
BVAL476
BTYR478
BGLY488
BVAL489
BALA490
BTHR491
BTRP677
BNAP753
site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAP B 753
ChainResidue
BARG298
BGLY534
BTHR535
BCYS566
BARG567
BSER596
BARG597
BLYS602
BTYR604
BGLN606
BASN635
BASP639
BTRP677
BSER678
BFAD752
site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE FAD C 752
ChainResidue
CARG424
CARG454
CTYR455
CTYR456
CSER457
CCYS472
CALA473
CVAL474
CVAL476
CTYR478
CLYS487
CGLY488
CVAL489
CALA490
CTHR491
CTHR535
CTRP677
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues144
DetailsDomain: {"description":"Flavodoxin-like","evidences":[{"source":"HAMAP-Rule","id":"MF_03212","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues59
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 Residues1
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 Residues6
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 Residues3
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 Residues6
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_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
AASP675
ASER457
ACYS630
site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
BASP675
BSER457
BCYS630
site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
CASP675
CSER457
CCYS630
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
ATYR456
site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
BTYR456
site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
CTYR456
site_idMCSA1
Number of Residues4
DetailsM-CSA 117
ChainResidueDetails
ASER457hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser
ACYS630electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction
AASP675hydrogen bond acceptor, modifies pKa
ATRP677steric role
site_idMCSA2
Number of Residues4
DetailsM-CSA 117
ChainResidueDetails
BSER457hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser
BCYS630electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction
BASP675hydrogen bond acceptor, modifies pKa
BTRP677steric role
site_idMCSA3
Number of Residues4
DetailsM-CSA 117
ChainResidueDetails
CSER457hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser
CCYS630electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction
CASP675hydrogen bond acceptor, modifies pKa
CTRP677steric role

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