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Ligands
Code Name Style Show Link
ZN Zinc ion
LSS 5'-O-(L-leucylsulfamoyl)adenosine
9YN (2~{S})-~{N}-[(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-(hydroxymethyl)-4-oxidanyl-oxolan-3-yl]-2-azanyl-4-methyl-pentanamide
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Glycosylation
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Code : 5ON3   PDBj   RCSB PDB   PDBe
Header : LIGASE
Title : Quaternary complex of mutant T252A of E. coli leucyl-tRNA synthetase with tRNA(leu), leucyl-adenylate analogue, and post-transfer editing analogue of leucine in the aminoacylation conformation
Release Data : 2017-11-15
Compound :
mol_id molecule chains synonym
1 Leucine--tRNA ligase A,D Leucyl-tRNA synthetase,LeuRS
ec: 6.1.1.4
mutation: T252A
mol_id molecule chains
2 tRNA(leu) B,E
Source :
mol_id organism_scientific expression_system
1 Escherichia coli K-12  (taxid:83333) Escherichia coli BL21  (taxid:511693)
gene: leuS, b0642, JW0637
mol_id organism_scientific
2 Escherichia coli  (taxid:562)
synthetic: yes
other_details: T7 in vitro transcribed
Authors : Palencia, A., Cusack, S.
Keywords : reaction catalysed: ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu) protein translation, aminoacyl-tRNA activity, leucine-tRNA ligase, class Ia, TRANSLATION, LIGASE
Exp. method : X-RAY DIFFRACTION ( 3.10 Å )
Citation :

Kinetic Origin of Substrate Specificity in Post-Transfer Editing by Leucyl-tRNA Synthetase.

Dulic, M.,Cvetesic, N.,Zivkovic, I.  et al.
(2018)  J. Mol. Biol.  430 : 1 - 16

PubMed: 29111343
DOI: 10.1016/j.jmb.2017.10.024

Chain : A, D
UniProt : P07813 (SYL_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl- tRNA(Leu) 6.1.1.4 HAMAP-Rule:MF_00049
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