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Structure of IDP01650

2.0 Angstrom Resolution Crystal Structure of Glucose-6-phosphate Isomerase (pgi) from Bacillus anthracis.

Edit deposit information
CSGID target
IDP01650 
PDB Id
3IFS (NCBI MMDB
Authors
'G.Minasov,Z.Wawrzak,O.Onopriyenko,E.Gordon,S.N.Peterson,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)' 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
Jul 24, 2009 
Release Date
Aug 11, 2009 

Annotation

Description
Glucose-6-phosphate isomerase, or phosphoglucose isomerase, is an enzyme that catalyzes the reversible interconversion of glucose-6-phosphate into fructose-6-phosphate in the second step of of the Embden-Meyerhof glycolytic pathway. There is evidence that phosphoglucose isomerase acts as a molecular messenger. It is produced and secreted by white blood cells, and acts to regulate the growth of several different cell types. A deficiency of phosphoglucose isomerase is responsible for the hemolytic anemias. The functional form of the Glucose-6-phosphate isomerase is a dimer. Each molecule is divided into two globular domains and a C-terminal tail. Both domains have a central core of a beta pleated sheet flanked by α-helices to form a typical alpha/beta folding motif. The active site is situated in a cleft between the large and small domains of the monomer and is formed by the association of the two subunits. There are several Glucose-6-phosphate isomerases from different organisms reported by the CSGID: from Vibrio cholerae (idp01329), Bacillus anthracis (idp01650) and Staphylococcus aureus (idp00736).  
Functional assignment
Glucose-6-phosphate isomerase 

Ligands

Ligand code Name Ligand type
CL CHLORIDE ION crystallization
SO4 sulfate molecule crystallization
PGE crystallization
LI lithium ion
MSE modified residue

Structure information

Unit cell parameters

Space Group
P 21 21 2  
Unit Cell

a=111.80Å, b=303.64Å, c=72.09Å
α=90.00, β=90.00, γ=90.00 
Solvent content
38.36  
Matthews coefficient
2  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.87-2.00Å (2.06-2.00Å)  
Rall(%)
14.3 
Rwork(%)
14.0 (16.5) 
Rfree(%)
19.0 (22.4) 
Num. observed reflections
163286 (11229) 
Num. Rfree reflections
8164 (575) 
Completeness(%)
98.7 (93.3) 

Model parameters

Num Atoms
21772  
Num Waters
2356  
Num Hetatoms
2450  
Model mean isotropic B factor
14.090Å2  
RMSD bond length
0.011Å  
RMSD bond angle
1.406°  
Filename uploaded
idp01650-3.pdb (uploaded on Jul 24, 2009 11:46 PM)  
Inserted
Jul 24, 2009