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1PXG

Crystal structure of the mutated tRNA-guanine transglycosylase (TGT) D280E complexed with preQ1

Functional Information from GO Data
ChainGOidnamespacecontents
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
A0008616biological_processqueuosine biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046872molecular_functionmetal ion binding
A0101030biological_processtRNA-guanine transglycosylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
ACYS318
ACYS320
ACYS323
AHIS349

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PRF A 401
ChainResidue
AGLY230
ALEU231
AVAL233
AMET260
AHOH516
ATYR106
AASP156
ACYS158
AGLN203
AGLY229

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1001
ChainResidue
APRO56
AGLU57
AGLY94
ATRP95
AASP96
AARG97

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1002
ChainResidue
AARG11
AMET32
ALYS33
AARG34
AGLY35
AVAL36
AHOH658
AHOH705
AHOH761

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1003
ChainResidue
APHE16
ASER17
AILE18
AASP254
AHOH691
AHOH729

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1004
ChainResidue
APRO78
AHIS333
AARG336
AALA337
AHOH640
AHOH743

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1005
ChainResidue
AGLU317
ALYS360
APHE373
AARG380
AHOH521
AHOH773

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1006
ChainResidue
AGLN117
ASER118
AARG174
APRO252
AASP254
ALYS255
AHOH783
AHOH785

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 1007
ChainResidue
AALA61
ATHR62
ACYS320
AALA321
AGLU348
AHOH772

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 1008
ChainResidue
AARG38
AARG60
AGLY63

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492
ChainResidueDetails
ASER103

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000305|PubMed:12949492
ChainResidueDetails
ACYS281

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:12949492
ChainResidueDetails
ASER103
AGLU157
AGLY204
ALEU231

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00168, ECO:0000269|PubMed:10413112, ECO:0000269|PubMed:11178905, ECO:0000269|PubMed:11921407, ECO:0000269|PubMed:12646024, ECO:0000269|PubMed:12909636, ECO:0000269|PubMed:12949492, ECO:0000269|PubMed:14523925, ECO:0000269|PubMed:19627989, ECO:0000269|PubMed:8654383, ECO:0000269|PubMed:8961936
ChainResidueDetails
AHIS319
AALA321
AGLN324
AASN350

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pud
ChainResidueDetails
AASP102

site_idMCSA1
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
ASER103proton shuttle (general acid/base)
ACYS281covalent catalysis
AHIS319metal ligand
AALA321metal ligand
AGLN324metal ligand
AASN350metal ligand

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PDB entries from 2024-07-10

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