5pgm
From Proteopedia
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SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE
Overview
The structure of a new crystal form of Saccharomyces cerevisiae, phosphoglycerate mutase has been solved and refined to 2.12 A with working, and free R-factors of 19.7 and 22.9 %, respectively. Higher-resolution, data and greater non-crystallographic symmetry have produced a more, accurate protein structure than previously. Prominent among the, differences from the previous structure is the presence of two sulphate, ions within each active site cleft. The separation of the sulphates, suggests that they may occupy the same sites as phospho groups of the, bisphosphate ligands of the enzyme. Plausible binding modes for, 2,3-bisphosphoglycerate and 1, 3-bisphosphoglycerate are thereby, suggested. These results support previous conclusions from mutant studies, highlight interesting new targets ... [(full description)]
About this Structure
5PGM is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with SO4 and ALA as [ligands]. Active as [[1]], with EC number [5.4.2.1]. Full crystallographic information is available from [OCA].
Reference
Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism., Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA, J Mol Biol. 1999 Mar 12;286(5):1507-17. PMID:10064712
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