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PDBsum entry 4j75

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protein ligands Protein-protein interface(s) links
Ligase PDB id
4j75

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
374 a.a.
Ligands
TYM ×2
GOL ×2
Waters ×213
PDB id:
4j75
Name: Ligase
Title: Crystal structure of a parasite tRNA synthetase, product-bound
Structure: Tryptophanyl-tRNA synthetase. Chain: a, b. Fragment: unp residues 229-632. Synonym: tryptophan--tRNA ligase. Engineered: yes
Source: Plasmodium falciparum. Organism_taxid: 36329. Strain: 3d7. Gene: pf13_0205. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.40Å     R-factor:   0.194     R-free:   0.223
Authors: C.Y.Koh,J.E.Kim,C.L.M.J.Verlinde,W.G.J.Hol
Key ref: C.Y.Koh et al. (2013). Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design. Mol Biochem Parasitol, 189, 26-32. PubMed id: 23665145 DOI: 10.1016/j.molbiopara.2013.04.007
Date:
12-Feb-13     Release date:   22-May-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8IDW3  (Q8IDW3_PLAF7) -  tryptophan--tRNA ligase from Plasmodium falciparum (isolate 3D7)
Seq:
Struc:
 
Seq:
Struc:
632 a.a.
374 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.1.1.2  - tryptophan--tRNA ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: tRNA(Trp) + L-tryptophan + ATP = L-tryptophyl-tRNA(Trp) + AMP + diphosphate + H+
tRNA(Trp)
+ L-tryptophan
+ ATP
= L-tryptophyl-tRNA(Trp)
Bound ligand (Het Group name = TYM)
matches with 62.16% similarity
+ AMP
+ diphosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1016/j.molbiopara.2013.04.007 Mol Biochem Parasitol 189:26-32 (2013)
PubMed id: 23665145  
 
 
Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design.
C.Y.Koh, J.E.Kim, A.J.Napoli, C.L.Verlinde, E.Fan, F.S.Buckner, W.C.Van Voorhis, W.G.Hol.
 
  ABSTRACT  
 
No abstract given.

 

 

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