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5YYM

Crystal structures of E.coli arginyl-trna synthetase (argrs) in complex with substrate Arg

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
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004814molecular_functionarginine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006420biological_processarginyl-tRNA aminoacylation
B0016874molecular_functionligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue ARG A 1001
ChainResidue
AASP118
AALA121
ASER135
AHIS158
ATYR336
AILE337
AASP338
AHOH1111
AHOH1280

site_idAC2
Number of Residues10
Detailsbinding site for residue ARG B 1001
ChainResidue
BASP118
BALA121
BPRO122
BASN123
BHIS158
BGLY160
BGLU258
BILE337
BHOH1122
BHOH1147

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 Residues20
DetailsMotif: {"description":"'HIGH' region"}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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