Center for Structural Genomics of Infectious Diseases

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Structure of IDP90717

CSGID target: IDP90717
PDB Id: 3Q3V (NCBI MMDB)
Authors: E.V.Filippova,Z.Wawrzak,O.Onopriyenko,A.Edwards,A.Savchenko,W.F.Anderson,Center For Structural Genomics Of Infectious Diseases (Csgid)
Responsible person: Ekaterina Filippova
Responsible lab: Northwestern University
Deposition Date: Dec 22, 2010
Release Date: Jan 12, 2011

Description: Phosphoglycerate kinase (PGK) is a key glycolytic enzyme that catalyzes the reversible transfer of a phosphate from 1,3-bisphosphoglycerate to ADP to form 3-phosphoglycerate and ATP in the presence of magnesium. PGK is essential in most living cells both for ATP generation in the glycolytic pathway of aerobes and for fermentation in anaerobes. The structure of PGK from Campylobacter jejuni has been determined to 2.15 A resolution. Like other kinases, PGK folds into two distinct domains, which undergo a large hinge-bending motion upon catalysis. The substrate binding sites, as deduced from electron density maps, are compatible with known substrate specificity and the stereochemical requirements for the enzymic reaction. The sulfate ion is found in the active site of the protein.
Functional assignment

Ligand code	Name	Ligand type
SO4	sulfate	biological
FMT	formate	crystallization
MSE		modified residue
K		crystallization
175	3,5-dihydro-5-methylidene-4h-imidazol-4-on