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1GLN

ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA SYNTHETASE

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 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 Residues8
DetailsBINDING:
ChainResidueDetails
AARG5
AHIS15
AGLU41
ATYR187
AARG205
AGLU208
ALEU236
ALYS243

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00022
ChainResidueDetails
ALYS246

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Interaction with tRNA; via carbonyl oxygen
ChainResidueDetails
ALEU354

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Essential for discrimination between tRNA(Glu) and tRNA(Gln)
ChainResidueDetails
AARG358

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

218853

PDB entries from 2024-04-24

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