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=114.27Å, b=114.27Å, c=83.72Å
α=90.00, β=90.00, γ=120.00 

Solvent content

51.72  

Matthews coefficient

2.55  

Refinement

Data for the highest resolution shell is in parentheses.

Resolution range

32.10-1.65Å (1.69-1.65Å)  

R_all(%)

13.2 

R_work(%)

13.1 (28.0) 

R_free(%)

16.0 (31.5) 

Num. observed reflections

75874 (5453) 

Num. R_free reflections

3793 (290) 

Completeness(%)

99.7 (98.4) 

Model parameters

Num Atoms

5169  

Num Waters

503  

Num Hetatoms

0  

Model mean isotropic B factor

13.460Ų  

RMSD bond length

0.017Å  

RMSD bond angle

1.453°  

Filename uploaded

idp02733_f6p.pdb (uploaded on Mar 12, 2010 5:36 PM)  

Inserted

Mar 12, 2010