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Structure of IDP01329

1.5 Angstrom Crystal Structure of Glucose-6-phosphate Isomerase from Vibrio cholerae.

Edit deposit information
CSGID target
IDP01329 
PDB Id
3HJB (NCBI MMDB
Authors
G.Minasov,A.Halavaty,L.Shuvalova,I.Dubrovska,J.Winsor,L.Papazisi,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
George Minasov 
Responsible lab
Northwestern University 
Deposition Date
May 21, 2009 
Release Date
Jun 16, 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
CA
CL CHLORIDE ION
NA Sodium ion
PEG
PG4

Structure information

Unit cell parameters

Space Group
P 1 21 1  
Unit Cell

a=125.66Å, b=75.09Å, c=127.46Å
α=90.00, β=90.21, γ=90.00 
Solvent content
50.1  
Matthews coefficient
2.46  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
29.88-1.50Å (1.54-1.50Å)  
Rall(%)
12.8 
Rwork(%)
12.7 (18.4) 
Rfree(%)
15.1 (21.5) 
Num. observed reflections
369935 (24363) 
Num. Rfree reflections
18496 (1306) 
Completeness(%)
97.7 (87.4) 

Model parameters

Num Atoms
22629  
Num Waters
4071  
Num Hetatoms
0  
Model mean isotropic B factor
6.350Å2  
RMSD bond length
0.010Å  
RMSD bond angle
1.370°  
Filename uploaded
idp01329v-c.pdb (uploaded on May 26, 2009 1:34 PM)  
Inserted
May 26, 2009