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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1Q2R

Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate

Functional Information from GO Data
ChainGOidnamespacecontents
A0002099biological_processtRNA wobble guanine modification
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006400biological_processtRNA modification
A0008033biological_processtRNA processing
A0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
A0008616biological_processtRNA queuosine(34) biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0046872molecular_functionmetal ion binding
B0002099biological_processtRNA wobble guanine modification
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006400biological_processtRNA modification
B0008033biological_processtRNA processing
B0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
B0008616biological_processtRNA queuosine(34) biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0046872molecular_functionmetal ion binding
C0002099biological_processtRNA wobble guanine modification
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006400biological_processtRNA modification
C0008033biological_processtRNA processing
C0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
C0008616biological_processtRNA queuosine(34) biosynthetic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0046872molecular_functionmetal ion binding
D0002099biological_processtRNA wobble guanine modification
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006400biological_processtRNA modification
D0008033biological_processtRNA processing
D0008479molecular_functiontRNA-guanosine(34) queuine transglycosylase activity
D0008616biological_processtRNA queuosine(34) biosynthetic process
D0016740molecular_functiontransferase activity
D0016757molecular_functionglycosyltransferase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS318
ACYS320
ACYS323
AHIS349
site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 9DG A 387
ChainResidue
AILE201
AGLN203
AGLY229
AGLY230
AMET260
AASP102
ASER103
ATYR106
AASP156
ACYS158
site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 402
ChainResidue
BCYS318
BCYS320
BCYS323
BHIS349
site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 9DG B 387
ChainResidue
BASP102
BTYR106
BASP156
BCYS158
BILE201
BGLY230
BMET260
site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 403
ChainResidue
CCYS318
CCYS320
CCYS323
CHIS349
site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 9DG C 387
ChainResidue
CASP102
CSER103
CGLY105
CTYR106
CASP156
CCYS158
CILE201
CGLN203
CGLY229
CGLY230
CMET260
site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 404
ChainResidue
DCYS318
DCYS320
DCYS323
DHIS349
site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 9DG D 387
ChainResidue
DASP102
DTYR106
DASP156
DCYS158
DILE201
DGLN203
DGLY229
DGLY230
DMET260
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsRegion: {"description":"RNA binding","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsRegion: {"description":"RNA binding; important for wobble base 34 recognition","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00168","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10413112","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11178905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11921407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12646024","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12909636","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12949492","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14523925","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19627989","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8654383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8961936","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pud
ChainResidueDetails
AASP102
site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pud
ChainResidueDetails
BASP102
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pud
ChainResidueDetails
CASP102
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pud
ChainResidueDetails
DASP102
site_idMCSA1
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
CASP102proton shuttle (general acid/base)
CASP280covalent catalysis
CCYS318metal ligand
CCYS320metal ligand
CCYS323metal ligand
CHIS349metal ligand
site_idMCSA2
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
DASP102proton shuttle (general acid/base)
DASP280covalent catalysis
DCYS318metal ligand
DCYS320metal ligand
DCYS323metal ligand
DHIS349metal ligand
site_idMCSA3
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
site_idMCSA4
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails

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PDB entries from 2025-07-09

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