1one: Difference between revisions

Revision as of 15:22, 16 February 2009

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1one, resolution 1.80Å (default scene)

Ligands:

MG, PEP

Non-Standard Residues:

2PG

Activity:

Phosphopyruvate hydratase, with EC number 4.2.1.11

Structural annotation:
Resources:	CATH : 1Onea01, 1Onea02, 1Oneb02, 1Oneb01 InterPro : Ipr000941 Pfam : PF03952, PF00113 SCOP : d1onea1, d1onea2, d1oneb1, d1oneb2 UniProt : P00924

Functional annotation:
Cellular component:	cytoplasm vacuole, cell cycle-correlated morphology phosphopyruvate hydratase complex mitochondrion
Biological process:	regulation of vacuole fusion, non-autophagic glycolysis gluconeogenesis
Molecular function:	protein binding phosphopyruvate hydratase activity metal ion binding lyase activity magnesium ion binding

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

YEAST ENOLASE COMPLEXED WITH AN EQUILIBRIUM MIXTURE OF 2'-PHOSPHOGLYCEATE AND PHOSPHOENOLPYRUVATE

Template:ABSTRACT PUBMED 8605183

About this Structure

1ONE is a 2 chains structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Larsen TM, Wedekind JE, Rayment I, Reed GH. A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution. Biochemistry. 1996 Apr 9;35(14):4349-58. PMID:8605183 doi:https://dx.doi.org/10.1021/bi952859c

Page seeded by OCA on Mon Feb 16 17:22:38 2009

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OCA

[1] Larsen TM, Wedekind JE, Rayment I, Reed GH. A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution. Biochemistry. 1996 Apr 9;35(14):4349-58. PMID:8605183 doi:https://dx.doi.org/10.1021/bi952859c

@@ Line 20: / Line 20: @@
 ==About this Structure==
-ONE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONE OCA].
+ONE is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONE OCA].
 ==Reference==
-A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution., Larsen TM, Wedekind JE, Rayment I, Reed GH, Biochemistry. 1996 Apr 9;35(14):4349-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8605183 8605183]
+<ref group="xtra">PMID:8605183</ref><references group="xtra"/>
 [[Category: Phosphopyruvate hydratase]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
 [[Category: Larsen, T M.]]
 [[Category: Rayment, I.]]
@@ Line 34: / Line 33: @@
 [[Category: Lyase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:45:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:22:38 2009''

1one: Difference between revisions

Revision as of 15:22, 16 February 2009

YEAST ENOLASE COMPLEXED WITH AN EQUILIBRIUM MIXTURE OF 2'-PHOSPHOGLYCEATE AND PHOSPHOENOLPYRUVATE

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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