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1TYB

STRUCTURAL ANALYSIS OF A SERIES OF MUTANTS OF TYROSYL-TRNA SYNTHETASE: ENHANCEMENT OF CATALYSIS BY HYDROPHOBIC INTERACTIONS

Functional Information from GO Data
ChainGOidnamespacecontents
E0000166molecular_functionnucleotide binding
E0004812molecular_functionaminoacyl-tRNA ligase activity
E0004831molecular_functiontyrosine-tRNA ligase activity
E0005524molecular_functionATP binding
E0006418biological_processtRNA aminoacylation for protein translation
E0006437biological_processtyrosyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TYR E 320
ChainResidue
ETYR34
EGLN195
EHOH349
EGLY36
EASP38
ELEU68
ETHR73
EASP78
ETYR169
EGLN173
EASP176

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues11
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHIGHL
ChainResidueDetails
EPRO39-LEU49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:1TYD
ChainResidueDetails
ETYR34
ETYR169

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250, ECO:0007744|PDB:1TYD
ChainResidueDetails
EGLN173
EASP176

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ELYS233

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
ELYS233
ELYS230

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1d2r
ChainResidueDetails
EARG86
ELYS82
ELYS233
ELYS230

site_idMCSA1
Number of Residues10
DetailsM-CSA 197
ChainResidueDetails

237992

PDB entries from 2025-06-25

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