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1Q11

Crystal structure of an active fragment of human tyrosyl-tRNA synthetase with tyrosinol

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004831molecular_functiontyrosine-tRNA ligase activity
A0005524molecular_functionATP binding
A0006418biological_processtRNA aminoacylation for protein translation
A0006437biological_processtyrosyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
AHIS305
APRO306
AGLY307
AASP308
AHOH1044
AHOH1186
AHOH1263

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 701
ChainResidue
ATHR45
ATYR52
ATYR97
AHOH1011
ATHR42
AALA43

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE TYE A 401
ChainResidue
ATYR39
AGLY41
ALEU72
AALA74
AHIS77
AVAL152
ATYR166
AGLN170
AASP173
AGLN182
AGLN188
AHOH1165

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 601
ChainResidue
AHIS12
AARG16
AHOH1155

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 602
ChainResidue
ALYS127
AGLU128
AHIS143
ALYS146

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:25533949, ECO:0007744|PDB:4Q93
ChainResidueDetails
ATYR39
AGLN170
AASP173

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:14671330, ECO:0007744|PDB:4QBT
ChainResidueDetails
ATYR166
AGLN188

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AMET1

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylglycine; in Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed => ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330
ChainResidueDetails
AGLY2

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS197
ALYS206

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER205

218853

PDB entries from 2024-04-24

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