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Structure of IDP02733

Glucose-6-phosphate isomerase from Francisella tularensis complexed with ribose 1,5-bisphosphate.

Edit deposit information
CSGID target
IDP02733 
PDB Id
3Q88 (NCBI MMDB
Authors
J.Osipiuk,N.Maltseva,J.Hasseman,W.F.Anderson,A.Joachimiak,Center For Structural Genomics Of Infectious Diseases (Csgid) 
Responsible person
Jerzy Osipiuk 
Responsible lab
Argonne National Laboratory 
Deposition Date
Jan 06, 2011 
Release Date
Jan 19, 2011 

Annotation

Description
Glucose-6-phosphate isomerase (also known as phosphoglucose isomerase (PGI)) is an enzyme that catalyzes the reversible aldose-ketose isomerization of glucose 6-phosphate (G6P) to fructose 6-phosphate (F6P). The reaction has direct roles in glycolysis and gluconeogenesis and, indirectly, other branches of carbohydrate metabolism such as the pentose phosphate pathway. PGI belongs to the aldose-ketose isomerase family of enzymes, all of which transfer a hydrogen atom between C1 and C2 of their respective substrates. PGIs use sugar substrates that exist in solution overwhelmingly in the hemiacetal or hemiketal ring form. PGIs also have a number of ‘moonlighting’ functions: it acts as an autocrine motility factor (AMF) and neuroleukin agent (NLK), a serine proteinase inhibitor and a differentiation and maturation mediator (DMM). It was found that GPI plays an essential role in the development of arthritis in mammals and may play roles in both cancer and autoimmunity.  
Functional assignment
Isomerase 

Ligands

Ligand code Name Ligand type
IPA crystallization
PO4 PHOSPHATE ION crystallization
MES 2-(n-morpholino)-ethanesulfonic acid crystallization
RI2 1,5-di-o-phosphono-alpha-d-ribofuranose biological
175 3,5-dihydro-5-methylidene-4h-imidazol-4-on

Structure information

Unit cell parameters

Space Group
P 32 2 1  
Unit Cell

a=114.47Å, b=114.47Å, c=84.50Å
α=90.00, β=90.00, γ=120.00 
Solvent content
52.69  
Matthews coefficient
2.6  

Refinement

Data for the highest resolution shell is in parentheses.
Resolution range
33.99-1.70Å (1.74-1.70Å)  
Rall(%)
14.8 
Rwork(%)
14.6 (28.7) 
Rfree(%)
17.4 (34.0) 
Num. observed reflections
70373 (5069) 
Num. Rfree reflections
3518 (279) 
Completeness(%)
99.7 (98.2) 

Model parameters

Num Atoms
5214  
Num Waters
483  
Num Hetatoms
0  
Model mean isotropic B factor
14.050Å2  
RMSD bond length
0.019Å  
RMSD bond angle
1.695°  
Filename uploaded
idp02733_prp.pdb (uploaded on Jan 06, 2011 1:32 PM)  
Inserted
Jan 06, 2011