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Ligands
Code Name Style Show Link
91Y 3-[(cyclohexanecarbonyl)amino]-N-(2,3-dihydro-1h-inden-2-yl)pyrazine-2-carboxamide
PRO Proline
ZN Zinc ion
Non-standard Residues
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Glycosylation
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Code : 5VAD   PDBj   RCSB PDB   PDBe
Header : LIGASE/LIGASE inhibitor
Title : Crystal structure of human Prolyl-tRNA synthetase (PRS) in complex with inhibitor
Release Data : 2017-05-31
Compound :
mol_id molecule chains synonym
1 Bifunctional glutamate/proline--tRNA ligase A,B Bifunctional aminoacyl-tRNA synthetase,Cell proliferation-inducing gene 32 protein,Glutamatyl-prolyl-tRNA synthetase
ec: 6.1.1.17,6.1.1.15
fragment: UNP residues 998-1512
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: EPRS, GLNS, PARS, QARS, QPRS, PIG32
Authors : Okada, K., Skene, R.J.
Keywords : aminoacyl-tRNA synthetase, ATP dependent, inhibitor, LIGASE-LIGASE inhibitor complex
Exp. method : X-RAY DIFFRACTION ( 2.3600 Å )
Citation :

Discovery of a novel prolyl-tRNA synthetase inhibitor and elucidation of its binding mode to the ATP site in complex with l-proline.

Adachi, R.,Okada, K.,Skene, R.  et al.
(2017)  Biochem. Biophys. Res. Commun.  488 : 393 - 399

PubMed: 28501621
DOI: 10.1016/j.bbrc.2017.05.064

Chain : A, B
UniProt : P07814 (SYEP_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L- glutamyl-tRNA(Glu) 6.1.1.17 PubMed:3290852
left-to-right
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl- tRNA(Pro) 6.1.1.15 PubMed:23263184, PubMed:24100331, PubMed:29576217, PubMed:37212275
left-to-right PubMed:24100331