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1J09

Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP and 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
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AATP501
AHOH1395
AHOH1396
AHOH1397

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GLU A 500
ChainResidue
AASN191
AARG205
ATRP209
AATP501
AHOH1021
AHOH1028
AHOH1138
AARG5
AALA7
ASER9
AGLU41
ATYR187

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE ATP A 501
ChainResidue
AHIS15
AGLU208
ATRP209
ALEU235
ALEU236
ALYS243
AILE244
ASER245
ALYS246
AARG247
AGLU500
AMG502
AHOH1037
AHOH1072
AHOH1085
AHOH1147
AHOH1185
AHOH1270
AHOH1359
AHOH1395
AHOH1396
AHOH1397

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PspTGdPHVGTA
ChainResidueDetails
APRO8-ALA19

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsRegion: {"description":"Interaction with tRNA"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues15
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Interaction with tRNA; via carbonyl oxygen"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Essential for discrimination between tRNA(Glu) and tRNA(Gln)"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 12554668
ChainResidueDetails
ALYS246

site_idMCSA1
Number of Residues1
DetailsM-CSA 318
ChainResidueDetails
ALYS246attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity

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PDB entries from 2025-10-29

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