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1TKG

Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with an analog of seryladenylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0005524molecular_functionATP binding
A0043039biological_processtRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SSA A 500
ChainResidue
AHIS73
APRO170
AGLY171
AASP180
AMET181
ACYS182
AARG183
AHOH508
AHOH517
AHOH611
AALA76
AHIS77
AILE94
AGLY95
APRO96
ATYR104
AILE159
ALYS169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues60
DetailsDomain: {"description":"TGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU01228","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues223
DetailsRegion: {"description":"Correctly edits mischarged seryl-tRNA(Thr)","evidences":[{"source":"PubMed","id":"15525511","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues61
DetailsRegion: {"description":"N1 domain","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues161
DetailsRegion: {"description":"N2 domain, the editing domain","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues19
DetailsRegion: {"description":"tRNA acceptor stem binding","evidences":[{"source":"PubMed","id":"10319817","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 540
ChainResidueDetails

246905

PDB entries from 2025-12-31

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