3pgm
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:3pgm.gif|left|200px]] | + | [[Image:3pgm.gif|left|200px]] |
| - | + | ||
| - | '''THE STRUCTURE OF YEAST PHOSPHOGLYCERATE MUTASE AT 0.28 NM RESOLUTION''' | + | {{Structure |
| + | |PDB= 3pgm |SIZE=350|CAPTION= <scene name='initialview01'>3pgm</scene>, resolution 2.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE STRUCTURE OF YEAST PHOSPHOGLYCERATE MUTASE AT 0.28 NM RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 3PGM is a [ | + | 3PGM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry 1PGM. The following page contains interesting information on the relation of 3PGM with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb50_1.html The Glycolytic Enzymes]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PGM OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/6115412 6115412] |
[[Category: Phosphoglycerate mutase]] | [[Category: Phosphoglycerate mutase]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| Line 23: | Line 32: | ||
[[Category: transferase (phosphoryl)]] | [[Category: transferase (phosphoryl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:06:37 2008'' |
Revision as of 17:06, 20 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Phosphoglycerate mutase, with EC number 5.4.2.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF YEAST PHOSPHOGLYCERATE MUTASE AT 0.28 NM RESOLUTION
Overview
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.
About this Structure
3PGM is a Single protein structure of sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entry 1PGM. The following page contains interesting information on the relation of 3PGM with [The Glycolytic Enzymes]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 19:06:37 2008
