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1EOV

FREE ASPARTYL-TRNA SYNTHETASE (ASPRS) (E.C. 6.1.1.12) FROM YEAST

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004815molecular_functionaspartate-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006418biological_processtRNA aminoacylation for protein translation
A0006422biological_processaspartyl-tRNA aminoacylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLY282
AALA326
AHIS334
AILE479
AGLY482
AILE486
ALEU529

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
APRO302

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
APRO503

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358
ChainResidueDetails
ALEU547

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
AARG325
AARG531
AASP342

site_idMCSA1
Number of Residues7
DetailsM-CSA 404
ChainResidueDetails
AARG325electrostatic stabiliser
AGLU327electrostatic stabiliser, metal ligand
AARG333electrostatic stabiliser, steric role
AHIS334electrostatic stabiliser, steric role
AGLU478electrostatic stabiliser, metal ligand
ASER481electrostatic stabiliser, metal ligand
AARG531electrostatic stabiliser, steric role

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PDB entries from 2025-06-18

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