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3FNR

CRYSTAL STRUCTURE OF PUTATIVE ARGINYL T-RNA SYNTHETASE FROM Campylobacter jejuni;

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004814molecular_functionarginine-tRNA ligase activity
A0005524molecular_functionATP binding
A0006418biological_processtRNA aminoacylation for protein translation
A0006420biological_processarginyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AHOH60
AGLY99
AGLU100
ALYS102
ALYS458
AHOH603
AHOH604

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
ATHR292
ATYR293
AHOH68
AARG286

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 3
ChainResidue
ALYS427
ATYR488
ALYS492
AVAL493
AVAL494
AHOH593

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
AGLY154
AASN155
AARG243
ATYR246

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 539
ChainResidue
AASP297
AHOH633

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..TGpLHIGHA
ChainResidueDetails
APRO115-ALA124

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1a8h
ChainResidueDetails
ALYS359

222036

PDB entries from 2024-07-03

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