3PGK

The structure of yeast phosphoglycerate kinase at 0.25 nm resolution

Replaces:  1PGK

Summary for 3PGK

• Entry DOI: 10.2210/pdb3pgk/pdb
• Descriptor: PHOSPHOGLYCERATE KINASE, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: phosphotransferase(carboxyl as acceptor), transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm : P00560
• Total number of polymer chains: 1
• Total formula weight: 45369.67

Authors

Shaw, P.J.,Walker, N.P.,Watson, H.C. (deposition date: 1982-07-15, release date: 1982-09-24, Last modification date: 2024-02-21)

Primary citation

Watson, H.C.,Walker, N.P.,Shaw, P.J.,Bryant, T.N.,Wendell, P.L.,Fothergill, L.A.,Perkins, R.E.,Conroy, S.C.,Dobson, M.J.,Tuite, M.F.
Sequence and structure of yeast phosphoglycerate kinase.
Embo J., 1:1635-1640, 1982

PubMed Abstract: The structure of yeast phosphoglycerate kinase has been determined with data obtained from amino acid sequence, nucleotide sequence, and X-ray crystallographic studies. The substrate binding sites, as deduced from electron density maps, are compatible with known substrate specificity and the stereochemical requirements for the enzymic reaction. A carboxyl-imidazole interaction appears to be involved in controlling the transition between the open and closed forms of the enzyme.

PubMed: 6765200

Experimental method

X-RAY DIFFRACTION (2.5 Å)