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1WKE

TRNA-GUANINE TRANSGLYCOSYLASE

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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
ACYS318
ACYS320
ACYS323
AHIS349

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
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 Residues4
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 Residues1
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 Residues1
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 Residues7
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 Residues4
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_idMCSA1
Number of Residues6
DetailsM-CSA 881
ChainResidueDetails
AASP102proton shuttle (general acid/base)
AASP280covalent catalysis
ACYS318metal ligand
ACYS320metal ligand
ACYS323metal ligand
AHIS349metal ligand

238582

PDB entries from 2025-07-09

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