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1AMO

THREE-DIMENSIONAL STRUCTURE OF NADPH-CYTOCHROME P450 REDUCTASE: PROTOTYPE FOR FMN-AND FAD-CONTAINING ENZYMES

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
B0003420biological_processregulation of growth plate cartilage chondrocyte proliferation
B0003958molecular_functionNADPH-hemoprotein reductase activity
B0004128molecular_functioncytochrome-b5 reductase activity, acting on NAD(P)H
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005829cellular_componentcytosol
B0007584biological_processresponse to nutrient
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
B0009812biological_processflavonoid metabolic process
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016787molecular_functionhydrolase activity
B0019395biological_processfatty acid oxidation
B0019899molecular_functionenzyme binding
B0022900biological_processelectron transport chain
B0032332biological_processpositive regulation of chondrocyte differentiation
B0043066biological_processnegative regulation of apoptotic process
B0043231cellular_componentintracellular membrane-bounded organelle
B0043602biological_processnitrate catabolic process
B0045542biological_processpositive regulation of cholesterol biosynthetic 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
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
B0090181biological_processregulation of cholesterol metabolic process
B0090346biological_processcellular organofluorine metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FAD A 750
ChainResidue
AHIS319
ATYR478
AGLY488
AVAL489
AALA490
ATHR491
AALA538
ATRP677
AHOH774
AHOH814
AARG424
AARG454
ATYR455
ATYR456
ASER457
ACYS472
AALA473
AVAL474

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
ASER86
AGLN87
ATHR88
AGLY89
ATHR90
AALA91
AALA138
ATHR139
ATYR140
AGLY141
AGLY143
ALEU173
AGLY174
AASN175
AHIS180
APHE181
AASN182
AASP208
ALEU212

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAP A 752
ChainResidue
AARG298
AGLY534
ATHR535
ACYS566
AARG567
ASER596
AARG597
ALYS602
ATYR604
AGLN606
AMET636
AASP639
AHOH767
AHOH807

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FAD B 750
ChainResidue
BHIS319
BARG424
BARG454
BTYR455
BTYR456
BSER457
BCYS472
BALA473
BVAL474
BTYR478
BGLY488
BVAL489
BALA490
BTHR491
BALA538
BTRP677
BHOH770
BHOH808

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN B 751
ChainResidue
BSER86
BGLN87
BTHR88
BGLY89
BTHR90
BALA91
BALA138
BTHR139
BTYR140
BGLY141
BGLY143
BLEU173
BGLY174
BASN175
BHIS180
BPHE181
BASN182
BASP208
BLEU212

site_idAC6
Number of Residues14
DetailsBINDING SITE FOR RESIDUE NAP B 752
ChainResidue
BASP639
BHOH763
BHOH801
BARG298
BGLY534
BTHR535
BCYS566
BARG567
BSER596
BARG597
BLYS602
BTYR604
BGLN606
BMET636

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
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
AGLY536
AARG597
AVAL603
ASER678
BGLN87
BTHR139
BGLY174
BTYR455
BGLU479
BVAL489
BGLY536
BARG597
BVAL603
BSER678
AGLN87
ATHR139
AGLY174
ATYR455
AGLU479
AVAL489

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:11371558, ECO:0000269|PubMed:21345800, ECO:0000269|PubMed:9237990
ChainResidueDetails
AASP209
BASP209

site_idSWS_FT_FI3
Number of Residues4
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
BHIS299
BVAL640
AHIS299
AVAL640

site_idSWS_FT_FI4
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|Ref.8
ChainResidueDetails
AARG425
BARG425

site_idSWS_FT_FI5
Number of Residues2
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
AALA473
BALA473

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 117
ChainResidueDetails
AILE458hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser
AGLY631electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction
AVAL676hydrogen bond acceptor, modifies pKa
ASER678steric role

site_idMCSA2
Number of Residues4
DetailsM-CSA 117
ChainResidueDetails
BILE458hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay, radical stabiliser
BGLY631electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay, steric role, van der waals interaction
BVAL676hydrogen bond acceptor, modifies pKa
BSER678steric role

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PDB entries from 2024-04-17

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