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2CFO

Non-Discriminating Glutamyl-tRNA Synthetase from Thermosynechococcus elongatus in Complex with Glu

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004818molecular_functionglutamate-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006424biological_processglutamyl-tRNA aminoacylation
A0008270molecular_functionzinc ion binding
A0016874molecular_functionligase activity
A0043039biological_processtRNA aminoacylation
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004818molecular_functionglutamate-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006424biological_processglutamyl-tRNA aminoacylation
B0008270molecular_functionzinc ion binding
B0016874molecular_functionligase activity
B0043039biological_processtRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GLU A1486
ChainResidue
AARG6
ATYR192
AVAL196
AARG210
AGLY211
AHIS214
AHOH2141

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PspTGnLHIGTA
ChainResidueDetails
APRO9-ALA20

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsMotif: {"description":"'HIGH' region"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"'KMSKS' region"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16876193","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j09
ChainResidueDetails
ALYS251

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j09
ChainResidueDetails
BLYS251

243531

PDB entries from 2025-10-22

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