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1N77

Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with tRNA(Glu) and ATP.

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 Residues15
DetailsBINDING SITE FOR RESIDUE ATP A 600
ChainResidue
APRO8
AGLU208
ATRP209
ALEU235
AILE244
AHOH1234
CA576
ASER9
ATHR11
AHIS15
AGLY17
ATHR18
AILE21
AARG47
AALA206

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP B 601
ChainResidue
BPRO8
BSER9
BHIS15
BTHR18
BILE21
BALA206
BGLU208
BTRP209
BLEU235
BLEU236
BILE244
BHOH1332
BHOH1456
DA576

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 Residues30
DetailsRegion: {"description":"Interaction with tRNA"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues30
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Interaction with tRNA; via carbonyl oxygen"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Essential for discrimination between tRNA(Glu) and tRNA(Gln)"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j09
ChainResidueDetails
ALYS246

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j09
ChainResidueDetails
BLYS246

site_idMCSA1
Number of Residues1
DetailsM-CSA 318
ChainResidueDetails

site_idMCSA2
Number of Residues1
DetailsM-CSA 318
ChainResidueDetails

246704

PDB entries from 2025-12-24

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