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Structure of IDP90735

Phosphopyruvate hydratase from Campylobacter jejuni.

Edit deposit information
CSGID target
IDP90735 
PDB Id
3QN3 (NCBI MMDB
Authors
J.Osipiuk,M.Gu,K.Kwon,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Feb 07, 2011 
Release Date
Feb 23, 2011 

Annotation

Description
Phosphopyruvate dehydratase, also known as enolase, is a metalloenzyme responsible for the formation of phosphoenolpyruvate (PEP) from 2-phosphoglycerate (2-PG), the ninth step of glycolysis. The enzyme can also catalyze the reverse reaction, depending on concentrations of substrates. Genes of the glycolysis pathway, including enolase gene, have been found to be overexpressed in several cancers. Several glycolytic inhibitors are currently in preclinical and clinical development for cancer treatment. 
Functional assignment
Dehydratase 

Ligands

Ligand code Name Ligand type
GOL crystallization
MPD crystallization
MG MAGNESIUM ION crystallization
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
I 2 2 2  
Unit Cell

a=120.47Å, b=148.89Å, c=234.72Å
α=90.00, β=90.00, γ=90.00 
Solvent content
 
Matthews coefficient
 

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
36.00-2.13Å (2.18-2.13Å)  
Rall(%)
17.8 
Rwork(%)
17.6 (25.8) 
Rfree(%)
21.6 (29.2) 
Num. observed reflections
113627 (7736) 
Num. Rfree reflections
5681 (368) 
Completeness(%)
96.3 (90.0) 

Model parameters

Num Atoms
13827  
Num Waters
775  
Num Hetatoms
0  
Model mean isotropic B factor
28.910Å2  
RMSD bond length
0.017Å  
RMSD bond angle
1.501°  
Filename uploaded
idp90735.pdb (uploaded on Feb 07, 2011 5:35 PM)  
Inserted
Feb 07, 2011