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4N9Q

Crystal structure of paAzoR1 bound to ubiquinone-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0003960molecular_functionNADPH:quinone reductase activity
A0009055molecular_functionelectron transfer activity
A0010181molecular_functionFMN binding
A0016491molecular_functionoxidoreductase activity
A0016652molecular_functionoxidoreductase activity, acting on NAD(P)H as acceptor
A0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
B0003960molecular_functionNADPH:quinone reductase activity
B0009055molecular_functionelectron transfer activity
B0010181molecular_functionFMN binding
B0016491molecular_functionoxidoreductase activity
B0016652molecular_functionoxidoreductase activity, acting on NAD(P)H as acceptor
B0016655molecular_functionoxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN A 301
ChainResidue
ASER10
APHE100
ASER145
AGLY147
AGLY148
APHE151
AGLU187
AHOH408
AHOH412
BVAL56
BPHE60
AARG12
ASER16
AGLN17
ASER18
APRO96
AMET97
ATYR98
AASN99

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE UQ1 A 302
ChainResidue
APHE60
APHE120
ATYR131
APHE173
BASN99
BPHE100
BFMN301

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ALEU48
AALA50
ASER104
AGLY105
BSER104

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AARG30
AARG40
AHOH429

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FMN B 301
ChainResidue
AUQ1302
BSER10
BARG12
BARG15
BSER16
BGLN17
BSER18
BPRO96
BMET97
BTYR98
BASN99
BPHE100
BSER145
BGLY147
BGLY148
BPHE151
BGLU187
BHOH406
BHOH413

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|PubMed:17904577, ECO:0000269|PubMed:20057057, ECO:0000269|PubMed:20417637, ECO:0000269|PubMed:22355582, ECO:0000269|PubMed:24915188, ECO:0007744|PDB:2V9C, ECO:0007744|PDB:3KEG, ECO:0007744|PDB:3LT5, ECO:0007744|PDB:3R6W, ECO:0007744|PDB:4N65, ECO:0007744|PDB:4N9Q
ChainResidueDetails
ASER10
ASER16
AMET97
ASER145
BSER10
BSER16
BMET97
BSER145

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:20417637, ECO:0000305|PubMed:22355582, ECO:0007744|PDB:3LT5, ECO:0007744|PDB:3R6W
ChainResidueDetails
AASN99
ATYR131
BASN99
BTYR131

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20417637, ECO:0000269|PubMed:22355582, ECO:0000269|PubMed:24915188, ECO:0007744|PDB:3LT5, ECO:0007744|PDB:3R6W, ECO:0007744|PDB:4N65, ECO:0007744|PDB:4N9Q
ChainResidueDetails
AGLU187
BGLU187

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:20057057, ECO:0000305|PubMed:20417637, ECO:0007744|PDB:3KEG, ECO:0007744|PDB:3LT5
ChainResidueDetails
AGLU188
BGLU188

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Important in the architecture of the active site => ECO:0000269|PubMed:20057057
ChainResidueDetails
ATYR131
BTYR131

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PDB entries from 2024-11-06

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