3pgm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 3pgm |SIZE=350|CAPTION= <scene name='initialview01'>3pgm</scene>, resolution 2.8Å | |PDB= 3pgm |SIZE=350|CAPTION= <scene name='initialview01'>3pgm</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3pgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pgm OCA], [http://www.ebi.ac.uk/pdbsum/3pgm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3pgm RCSB]</span> | |||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Watson, H C.]] | [[Category: Watson, H C.]] | ||
[[Category: Winn, S I.]] | [[Category: Winn, S I.]] | ||
[[Category: transferase (phosphoryl)]] | [[Category: transferase (phosphoryl)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:35:23 2008'' | ||
Revision as of 05:35, 31 March 2008
| |||||||
| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Phosphoglycerate mutase, with EC number 5.4.2.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE STRUCTURE OF YEAST PHOSPHOGLYCERATE MUTASE AT 0.28 NM RESOLUTION
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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 Mon Mar 31 05:35:23 2008