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9EF0

EM structure of cytochrome P450 reductase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003958molecular_functionNADPH-hemoprotein reductase activity
A0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
A0005737cellular_componentcytoplasm
A0005783cellular_componentendoplasmic reticulum
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
A0009812biological_processflavonoid metabolic process
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016787molecular_functionhydrolase activity
A0019395biological_processfatty acid oxidation
A0019899molecular_functionenzyme binding
A0022900biological_processelectron transport chain
A0032332biological_processpositive regulation of chondrocyte differentiation
A0043066biological_processnegative regulation of apoptotic process
A0043231cellular_componentintracellular membrane-bounded organelle
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
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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTOPO_DOM: Lumenal => ECO:0000255|HAMAP-Rule:MF_03212
ChainResidueDetails
AGLY2-LEU22

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_03212
ChainResidueDetails
APHE23-ILE43

site_idSWS_FT_FI3
Number of Residues634
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255|HAMAP-Rule:MF_03212
ChainResidueDetails
APHE44-SER678

site_idSWS_FT_FI4
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
ChainResidueDetails
ASER86
ATRP677
AALA138
ALEU173
AARG454
ATYR478
AGLY488
ATHR535
ASER596
ALYS602

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990
ChainResidueDetails
AASP208

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990
ChainResidueDetails
AARG298
AASP639

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:21345800, ECO:0000269|Ref.8
ChainResidueDetails
AARG424

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:19171935, ECO:0000269|PubMed:9237990, ECO:0000269|Ref.8
ChainResidueDetails
ACYS472

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N-acetylglycine => ECO:0000250|UniProtKB:P16435
ChainResidueDetails
AGLY2

Catalytic Information from CSA
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

237735

PDB entries from 2025-06-18

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