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1N75

Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with 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
A0043039biological_processtRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AATP501
AHOH1355
AHOH1356
AHOH1357

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP A 501
ChainResidue
ALEU236
ALYS243
AILE244
ASER245
ALYS246
AARG247
AMG502
AHOH1088
AHOH1098
AHOH1194
AHOH1267
AHOH1301
AHOH1355
AHOH1356
AHOH1357
AHIS15
AALA206
AGLU208
ATRP209
ALEU235

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_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1j09
ChainResidueDetails
ALYS246

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

226707

PDB entries from 2024-10-30

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