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2HL2

Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi in complex with an analog of seryladenylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0004829molecular_functionthreonine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
B0004829molecular_functionthreonine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SSA A 500
ChainResidue
AALA19
ALYS121
ALEU20
AILE43
AVAL45
ALEU88
AALA89
AALA94
APHE117
AGLY118

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SSA B 501
ChainResidue
AHOH1047
BALA19
BLEU20
BILE43
BVAL45
BPHE81
BALA82
BALA89
BALA94
BPHE117
BGLY118
BTYR120
BHOH1075

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues284
DetailsRegion: {"description":"Editing domain","evidences":[{"source":"HAMAP-Rule","id":"MF_00184","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15908961","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16902403","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"21098258","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26113036","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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