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1ZH6

Crystal Structure of p-acetylphenylalanine-tRNA synthetase in complex with p-acetylphenylalanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004831molecular_functiontyrosine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006437biological_processtyrosyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 4AF A 315
ChainResidue
AGLY34
ACYS159
AGLN173
ABME402
AGLU36
ALEU65
AALA67
AHIS70
AGLN109
ATYR151
AGLN155
AGLY158

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 402
ChainResidue
AGLY34
ACYS159
AVAL168
AHIS177
A4AF315

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME A 403
ChainResidue
AALA167
AHIS177
AALA180
AVAL188
ACYS190

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGkIHLGHY
ChainResidueDetails
APRO37-TYR46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:12754495
ChainResidueDetails
ALEU32
AGLU36
AGLN173

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
ASER207

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Interaction with t-RNA
ChainResidueDetails
AASN143

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ALYS204
ASER207

222415

PDB entries from 2024-07-10

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