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Phosphoglycerate Mutase 1

Cat. No.: CBCRY11
Background: The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as the cofactor. The crystal structures of human dPGM-B bound with citrate were determined in two crystal forms. These structures reveal a dimerization mode conserved in both of dPGM and BPGM (bisphosphoglycerate mutase), based on which a dPGM/BPGM heterodimer structure is proposed. Structural comparison supports that the conformational changes of residues 13-21 and 98-117 determine PGM/BPGM activity differences.
Protein Classification: isomerase hydrase
Structure Weight: 361525.84
Polymer: 1
Molecule: Phosphoglycerate mutase 1
Chain Length: 262 amino acids
PDB ID: 1YJX
MMDB ID: 33356
Source: E.coli
Method: X-Ray Diffraction
Resolution: 2.8?
Ligand Chemical Component: citric acid; chloride ion
Reference: Wang, Y., Wei, Z., Liu, L., Cheng, Z., Lin, Y., Ji, F., Gong, W.(2005) Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Biochem.Biophys.Res.Commun. 331: 1207-1215
Gene Name: PGAM1
Synonyms: PGAMA; PGAM-B; PGAM1; RP11-452K12.8; OTTHUMP00000020190; OTTHUMP00000059414; phosphoglycerate mutase A, nonmuscle form; EC 5.4.2.1,EC 5.4.2.4,EC 3.1.3.13; BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; phosphoglycerate mutase A, nonmuscle form
UniProt ID: P18669
Gene ID: 5223
Chromosome Location: 10q25.3
Function: bisphosphoglycerate 2-phosphatase activity; bisphosphoglycerate mutase activity; hydrolase activity; isomerase activity; phosphoglycerate mutase activity; protein kinase binding

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