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1H3E

Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with wild-type tRNAtyr(GUA) and with ATP and tyrosinol

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003723molecular_functionRNA binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004831molecular_functiontyrosine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006437biological_processtyrosyl-tRNA aminoacylation
A0016874molecular_functionligase activity
A0043039biological_processtRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP A 1433
ChainResidue
AGLY43
AGLY194
AGLN197
APRO222
ALEU223
ALEU224
ALYS232
AMET233
ASER234
ALYS235
ATYE1434
AALA44
AASP45
AHIS52
AGLY54
AHIS55
AVAL58
AARG93
AGLY193

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TYE A 1434
ChainResidue
ALYS41
AGLY43
AASP45
AASP85
ATYR175
AGLN179
AASP182
AGLU191
AGLN197
AATP1433

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS235

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ALYS232
ALYS235

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
AARG93
ALYS232
AARG89
ALYS235

237735

PDB entries from 2025-06-18

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