3pgm | pdb_00003pgm

THE STRUCTURE OF YEAST PHOSPHOGLYCERATE MUTASE AT 0.28 NM RESOLUTION

spinqualitylabelsall models 3pgm, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pgm is a 2 chain structure with sequence from Atcc 18824. This structure supersedes the now removed PDB entry 1pgm. The February 2004 RCSB PDB Molecule of the Month feature on The Glycolytic Enzymes by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 3PG, SO4 Activity: Phosphoglycerate mutase, with EC number 5.4.2.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PMG1_YEAST] Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of yeast phosphoglycerate mutase determined by X-ray crystallographic and amino acid sequence studies has been interpreted in terms of the chemical, kinetic and mechanistic observations made on this enzyme. There are two histidine residues at the active site, with imidazole groups almost parallel to each other and approximately 0.4 nm apart, positioned close to the 2 and 3 positions of the substrate. The simplest interpretation of the available information suggests that a ping-pong type mechanism operates in which at least one of these histidine residues participates in the phosphoryl transfer reaction. The flexible C-terminal region also plays an important role in the enzymic reaction. Structure and activity of phosphoglycerate mutase.,Winn SI, Watson HC, Harkins RN, Fothergill LA Philos Trans R Soc Lond B Biol Sci. 1981 Jun 26;293(1063):121-30. PMID:6115412 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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