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4N65

Crystal structure of paAzoR1 bound to anthraquinone-2-sulphonate

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, NAD(P) 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, NAD(P) 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 Residues20
DetailsBINDING SITE FOR RESIDUE FMN A 301
ChainResidue
ASER10
APHE100
ASER145
AARG146
AGLY147
AGLY148
APHE151
AGLU187
AGLU188
AHOH407
AHOH415
AARG12
BVAL56
ASER16
AGLN17
ASER18
APRO96
AMET97
ATYR98
AASN99

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE AQN A 302
ChainResidue
ATYR131
APHE173
AHOH514
AHOH531
BPHE100
BGLY147
BGLY148
BFMN301

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 303
ChainResidue
AARG30
AARG40

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AARG139
ALEU208
AALA212
AHOH459

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 305
ChainResidue
ALEU48
AALA50
ASER104
AGLY105
AHOH440
BLEU48
BSER104
BGLY105

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE FMN B 301
ChainResidue
APHE60
AAQN302
BSER10
BARG12
BSER16
BGLN17
BSER18
BPRO96
BMET97
BTYR98
BASN99
BPHE100
BSER145
BARG146
BGLY147
BGLY148
BPHE151
BHOH414
BHOH424
BHOH487
BHOH516

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BALA50
BVAL51
BTHR52
BPHE55
BASP74
BGLN112
BHOH404
BHOH412
BHOH437

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
BMET97
BSER145
ASER10
ASER16
AMET97
ASER145
BSER10
BSER16

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
BASN99
BTYR131
AASN99
ATYR131

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

221051

PDB entries from 2024-06-12

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