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PDBe Entry: 1wnz view

Isoleucyl-tRNA synthetase editing domain complexed with the post-transfer editing substrate analogue, Val-2AA
Summary
Header Ligasesearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.7 Å, R-factor: 21.0%, Free R-factor: 25.7%, Spacegroup: P 41 2 2
Released 25/10/2005, deposition: 11/08/2004, last revision: 24/02/2009
Authors Fukunaga, R.search; Yokoyama, S.search; RIKEN Structural Genomics/Proteomics Initiative (RSGI)search
Primary citation Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase
J.MOL.BIOL.search vol:359, pag:901-912 (2006) [PubMed ID 16697013 ]search
Keywords Ligasesearch, Structural Genomicssearch, NPPSFAsearch, National Project on Protein Structural and Functional Analysessearch, RIKEN Structural Genomics/Proteomics Initiativesearch, RSGIsearch
EC 6.1.1.5 ExPASy BRENDA search (A)
Organism Thermus thermophilus 274search(A)
UniProt Isoleucyl-tRNA synthetase (EC 6.1.1.5) (Isoleucine--tRNA ligase) (IleRS) P56690search (A)
Solvent A
Related entries 1wny
Polymers
Id Name Type UniProt Residues Observed
A isoleucyl-trna synthetase Protein P56690 (SYI_THET8)search
186 96%
Heterogens
Id Name Ligands
A 2'-(L-VALYL)AMINO-2'-DEOXYADENOSINE 2VA search
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