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4OBY

Crystal Structure of E.coli Arginyl-tRNA Synthetase and Ligand Binding Studies Revealed Key Residues in Arginine Recognition

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004814molecular_functionarginine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006420biological_processarginyl-tRNA aminoacylation
A0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ARG A 601
ChainResidue
AASP118
AGLN341
AALA121
AASN123
AHIS132
AHIS158
ATYR313
AASP317
ATYR335
AILE337

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PnvAKeMHVGHL
ChainResidueDetails
APRO122-LEU133

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsMotif: {"description":"'HIGH' region"}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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