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3OJW

Disulfide crosslinked cytochrome P450 reductase inactive

Functional Information from GO Data
ChainGOidnamespacecontents
A0003420biological_processregulation of growth plate cartilage chondrocyte proliferation
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
A0007584biological_processresponse to nutrient
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
A0045542biological_processpositive regulation of cholesterol biosynthetic 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
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
A0090181biological_processregulation of cholesterol metabolic process
A0090346biological_processcellular organofluorine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
AHOH50
ATYR140
AGLY141
AGLY143
ALEU173
AGLY174
AASN175
ATYR178
AHIS180
APHE181
AASN182
ASER86
AASP208
ALEU212
AVAL676
AGLN87
ATHR88
AGLY89
ATHR90
AALA91
AALA138
ATHR139

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE FAD A 752
ChainResidue
AHOH8
AHOH18
AHOH24
AHOH27
AHOH39
AHOH41
AHOH51
AHIS319
AARG424
AARG454
ATYR455
ATYR456
ASER457
ATHR472
AALA473
AVAL474
ATYR478
AGLY488
AVAL489
AALA490
ATHR491
ATRP677
AHOH741
AHOH793

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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
AALA91
AGLY143
ATYR178
AALA459
AGLY483
ATRP493
APHE540
AHIS601
AHIS607

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990
ChainResidueDetails
AGLU213

site_idSWS_FT_FI3
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
ALEU303
APHE644

site_idSWS_FT_FI4
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
AALA429

site_idSWS_FT_FI5
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
AGLU477

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 117
ChainResidueDetails
ASER462hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser
AASN635electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction

219140

PDB entries from 2024-05-01

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