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4ZAJ

2.2 Angstrom Crystal Structure of a Human Arginyl-tRNA Synthetase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004814molecular_functionarginine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006418biological_processtRNA aminoacylation for protein translation
A0006420biological_processarginyl-tRNA aminoacylation
Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PniAKeMHVGHL
ChainResidueDetails
APRO129-LEU140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsRegion: {"description":"Interaction with tRNA","evidences":[{"source":"UniProtKB","id":"Q05506","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues11
DetailsMotif: {"description":"'HIGH' region"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24859084","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Q2T","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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