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1N78

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

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
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
B0043039biological_processtRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG C 700
ChainResidue
CHOH2317
CHOH2318
CHOH2319
CHOH2320
CHOH2321
CHOH2322

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 701
ChainResidue
DHOH2326
DHOH2327
DHOH2328
DHOH2323
DHOH2324
DHOH2325

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE GOM A 600
ChainResidue
AARG5
AALA7
APRO8
ASER9
AGLY17
ATHR18
AILE21
AGLU41
ATYR187
AASN191
AARG205
AALA206
AGLU208
ATRP209
ALEU235
ALEU236
AILE244
AHOH1122
AHOH1294
AHOH1360
AHOH1480
CA576

site_idAC4
Number of Residues20
DetailsBINDING SITE FOR RESIDUE GOM B 601
ChainResidue
BARG5
BALA7
BSER9
BGLY17
BTHR18
BILE21
BGLU41
BTYR187
BASN191
BARG205
BALA206
BGLU208
BTRP209
BLEU235
BLEU236
BILE244
BHOH1137
BHOH1256
BHOH1624
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 Residues16
DetailsBINDING:
ChainResidueDetails
AARG5
BHIS15
BGLU41
BTYR187
BARG205
BGLU208
BLEU236
BLYS243
AHIS15
AGLU41
ATYR187
AARG205
AGLU208
ALEU236
ALYS243
BARG5

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00022
ChainResidueDetails
ALYS246
BLYS246

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with tRNA; via carbonyl oxygen
ChainResidueDetails
ALEU354
BLEU354

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Essential for discrimination between tRNA(Glu) and tRNA(Gln)
ChainResidueDetails
AARG358
BARG358

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
ALYS246attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity

site_idMCSA2
Number of Residues1
DetailsM-CSA 318
ChainResidueDetails
BLYS246attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase nucleophilicity

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PDB entries from 2024-10-16

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