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 

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)  

R_all(%)

14.8 

R_work(%)

14.6 (28.7) 

R_free(%)

17.4 (34.0) 

Num. observed reflections

70373 (5069) 

Num. R_free reflections

3518 (279) 

Completeness(%)

99.7 (98.2) 

Model parameters

Num Atoms

5214  

Num Waters

483  

Num Hetatoms

0  

Model mean isotropic B factor

14.050Ų  

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