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3PD5

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

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 Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 500
ChainResidue
ALYS16
AHOH3039
AHOH3049
BLYS128

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE TSB A 501
ChainResidue
AALA82
ALEU88
AALA89
AALA94
APHE117
AGLY118
ATYR120
AHOH3006
AHOH3007
AALA19
ALEU20
AILE43
AVAL45
APHE81

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TSB B 502
ChainResidue
BALA19
BLEU20
BILE43
BVAL45
BPHE81
BALA82
BLEU88
BALA89
BPHE117
BGLY118
BTYR120
BHOH3027
BHOH3028

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues142
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

245663

PDB entries from 2025-12-03

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