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1JA0

CYPOR-W677X

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
A0006809biological_processnitric oxide biosynthetic process
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
B0006809biological_processnitric oxide biosynthetic process
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 Residues23
DetailsBINDING SITE FOR RESIDUE FAD A 750
ChainResidue
AHIS319
AVAL476
ATYR478
AGLY488
AVAL489
AALA490
ATHR491
AALA538
ANAP752
AHOH805
AHOH807
AARG424
AHOH819
AHOH864
AHOH887
AHOH888
AARG454
ATYR455
ATYR456
ASER457
ACYS472
AALA473
AVAL474

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE FAD B 850
ChainResidue
BHIS319
BARG424
BARG454
BTYR455
BTYR456
BSER457
BCYS472
BALA473
BVAL474
BTYR478
BGLY488
BVAL489
BALA490
BTHR491
BNAP852
BHOH855
BHOH875
BHOH970

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FMN A 751
ChainResidue
ASER86
AGLN87
ATHR88
AGLY89
ATHR90
AALA91
AALA138
ATHR139
AGLY141
AGLY143
ALEU173
AGLY174
AASN175
ATYR178
AHIS180
APHE181
AASN182
AASP208
ALEU212
AVAL676
AHOH890

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR RESIDUE NAP A 752
ChainResidue
AARG298
ASER457
APRO533
AGLY534
ATHR535
ACYS566
ASER596
AARG597
ALYS602
ATYR604
AGLN606
ACYS630
AGLY631
AASP632
AASN635
AMET636
AASP639
AASP675
AVAL676
AFAD750
AHOH757
AHOH889

site_idAC5
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAP B 852
ChainResidue
BMET636
BASP639
BASP675
BVAL676
BFAD850
BHOH864
BHOH949
BHOH950
BARG298
BSER457
BGLY534
BTHR535
BCYS566
BARG567
BSER596
BARG597
BLYS602
BTYR604
BGLN606
BCYS630
BGLY631
BASP632
BASN635

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
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
BSER86
BALA138
BLEU173
BARG454
BTYR478
BGLY488
BTHR535
BSER596
BLYS602
AALA138
ALEU173
AARG454
ATYR478
AGLY488
ATHR535
ASER596
ALYS602

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
AASP208
BASP208

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
AARG298
AASP639
BARG298
BASP639

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
AARG424
BARG424

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
ACYS472
BCYS472

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 Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
ATYR456

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fnb
ChainResidueDetails
BTYR456

site_idMCSA1
Number of Residues3
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

site_idMCSA2
Number of Residues3
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

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PDB entries from 2024-11-06

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