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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 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