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PDBsum entry 3mav

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3mav
Jmol
Contents
Protein chains
348 a.a. *
Ligands
SO4 ×9
Waters ×370
* Residue conservation analysis
PDB id:
3mav
Name: Transferase
Title: Crystal structure of plasmodium vivax putative farnesyl pyro synthase (pv092040)
Structure: Farnesyl pyrophosphate synthase. Chain: a, b, c, d. Engineered: yes
Source: Plasmodium vivax. Organism_taxid: 126793. Strain: salvador i. Gene: pvx_092040. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.10Å     R-factor:   0.229     R-free:   0.262
Authors: A.Dong,J.Dunford,J.Lew,A.K.Wernimont,H.Ren,Y.Zhao,I.Koeierad U.Opperman,M.Sundstrom,J.Weigelt,A.M.Edwards,C.H.Arrowsmith A.Bochkarev,R.Hui,J.D.Artz,Structural Genomics Consortium (
Key ref: J.D.Artz et al. (2011). Molecular characterization of a novel geranylgeranyl pyrophosphate synthase from Plasmodium parasites. J Biol Chem, 286, 3315-3322. PubMed id: 21084289
Date:
24-Mar-10     Release date:   14-Apr-10    
Supersedes: 2ihi
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
A5K4U6  (A5K4U6_PLAVS) -  Farnesyl pyrophosphate synthase, putative
Seq:
Struc:
375 a.a.
348 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     isoprenoid biosynthetic process   1 term 
  Biochemical function     transferase activity     2 terms  

 

 
J Biol Chem 286:3315-3322 (2011)
PubMed id: 21084289  
 
 
Molecular characterization of a novel geranylgeranyl pyrophosphate synthase from Plasmodium parasites.
J.D.Artz, A.K.Wernimont, J.E.Dunford, M.Schapira, A.Dong, Y.Zhao, J.Lew, R.G.Russell, F.H.Ebetino, U.Oppermann, R.Hui.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22868759 J.A.Bell, K.L.Ho, and R.Farid (2012).
Significant reduction in errors associated with nonbonded contacts in protein crystal structures: automated all-atom refinement with PrimeX.
  Acta Crystallogr D Biol Crystallogr, 68, 935-952.  
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