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9Z2Y

Crystal structure of Glutamate-tRNA synthetase GluRS from Chlamydia pneumoniae in complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004818molecular_functionglutamate-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006424biological_processglutamyl-tRNA aminoacylation
A0016874molecular_functionligase activity
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004818molecular_functionglutamate-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006424biological_processglutamyl-tRNA aminoacylation
B0016874molecular_functionligase activity
Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PspTGdPHVGTA
ChainResidueDetails
APRO12-ALA23

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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