3pgk: Difference between revisions

[[Image:3pgk.gif|left|200px]]<br />

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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.

3PGK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG, ACE, ATP and 3PG as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1PGK. The following page contains interesting information on the relation of 3PGK with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3PGK OCA].  

[[Category: Shaw, P.J.]]

[[Category: Walker, N.P.]]

[[Category: Watson, H.C.]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:10:32 2007''