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2EL7

Crystal structure of Tryptophanyl-tRNA synthetase from Thermus thermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004830molecular_functiontryptophan-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006436biological_processtryptophanyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004830molecular_functiontryptophan-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006436biological_processtryptophanyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 1001
ChainResidue
AASP105
AGLU160

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGeIHIGNY
ChainResidueDetails
APRO10-TYR19

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ALYS195
ALYS198

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
BLYS195
BLYS198

227344

PDB entries from 2024-11-13

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