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3UXV

Crystal Structure of 7-cyano-7-deazaguanine reductase, QueF from Vibrio cholerae complexed with NADP and PreQ

Functional Information from GO Data
ChainGOidnamespacecontents
A0003674molecular_functionmolecular_function
A0005575cellular_componentcellular_component
A0005737cellular_componentcytoplasm
A0008150biological_processbiological_process
A0008616biological_processqueuosine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0033739molecular_functionpreQ1 synthase activity
A0046857molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
B0003674molecular_functionmolecular_function
B0005575cellular_componentcellular_component
B0005737cellular_componentcytoplasm
B0008150biological_processbiological_process
B0008616biological_processqueuosine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0033739molecular_functionpreQ1 synthase activity
B0046857molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
C0003674molecular_functionmolecular_function
C0005575cellular_componentcellular_component
C0005737cellular_componentcytoplasm
C0008150biological_processbiological_process
C0008616biological_processqueuosine biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0033739molecular_functionpreQ1 synthase activity
C0046857molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
D0003674molecular_functionmolecular_function
D0005575cellular_componentcellular_component
D0005737cellular_componentcytoplasm
D0008150biological_processbiological_process
D0008616biological_processqueuosine biosynthetic process
D0016491molecular_functionoxidoreductase activity
D0033739molecular_functionpreQ1 synthase activity
D0046857molecular_functionoxidoreductase activity, acting on other nitrogenous compounds as donors, with NAD or NADP as acceptor
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AHIS188
ASER204
AMSE284
AALA285
AARG286
AHOH311
AHOH371
BLEU139

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
ASER252
ASER273
AHIS274
CSER112
CASP114
CHOH337
AGLN251

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE NAP B 301
ChainResidue
ASER95
ALYS96
ALYS99
AGLN199
AARG262
AGLY263
BSER95
BLYS96
BLYS99
BARG262
BGLY263
BGUN300
BHOH325
BHOH686
BHOH719

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GUN B 300
ChainResidue
BTRP62
BLEU92
BILE93
BGLU94
BSER95
BPHE232
BHIS233
BGLU234
BILE267
BNAP301

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 302
ChainResidue
BALA126
BCYS127
BHOH326
BHOH414

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GUN C 300
ChainResidue
CTRP62
CLEU92
CILE93
CGLU94
CSER95
CPHE232
CHIS233
CGLU234
CILE267
DNAP301

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE NAP D 301
ChainResidue
CSER95
CLYS96
CLYS99
CARG262
CGLY263
CLEU265
CGUN300
DSER95
DLYS96
DLYS99
DARG262
DGLY263
DHOH332
DHOH717
DHOH718
DHOH824

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO D 302
ChainResidue
CLEU139
DHIS188
DSER204
DMSE284
DALA285
DARG286
DHOH293
DHOH466

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 303
ChainResidue
BSER112
BTRP113
BASP114
DGLN251
DSER252
DSER273
DHIS274

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL D 304
ChainResidue
AASN91
AHOH289
AHOH369
DPRO38
DASN91
DHOH312
DHOH393
DHOH471
DHOH607

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL D 305
ChainResidue
DHOH395
DHOH443
DHOH582
DGLU82
DGLU145
DASN281
DGLN282
DHOH374

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Thioimide intermediate => ECO:0000255|HAMAP-Rule:MF_00817, ECO:0000269|Ref.3
ChainResidueDetails
BALA194
CALA194
DALA194
AALA194

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00817
ChainResidueDetails
AASP201
BASP201
CASP201
DASP201

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING:
ChainResidueDetails
BILE93
BSER95
BHIS233
BARG262
CILE93
CSER95
CHIS233
CARG262
DILE93
DSER95
DHIS233
DARG262
AILE93
ASER95
AHIS233
AARG262

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PDB entries from 2024-06-12

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