PDBsum entry 3ph7

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Lyase PDB id
Protein chains
347 a.a. *
GRG ×4
Waters ×92
* Residue conservation analysis
PDB id:
Name: Lyase
Title: Crystal structure of plasmodium vivax putative polyprenyl pyrophosphate synthase in complex with geranylgeranyl dipho
Structure: Farnesyl pyrophosphate synthase. Chain: a, b, c, d. Engineered: yes
Source: Plasmodium vivax. Organism_taxid: 5855. Gene: pvx_092040. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.50Å     R-factor:   0.236     R-free:   0.273
Authors: A.K.Wernimont,J.Dunford,J.Lew,Y.Zhao,I.Kozieradzki,D.Cossar, M.Schapiro,A.Bochkarev,C.H.Arrowsmith,C.Bountra,J.Weigelt, A.M.Edwards,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
03-Nov-10     Release date:   17-Nov-10    
Supersedes: 3mys
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
A5K4U6  (A5K4U6_PLAVS) -  Farnesyl pyrophosphate synthase, putative
375 a.a.
347 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.
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.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.