3enl
From Proteopedia
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|PDB= 3enl |SIZE=350|CAPTION= <scene name='initialview01'>3enl</scene>, resolution 2.25Å | |PDB= 3enl |SIZE=350|CAPTION= <scene name='initialview01'>3enl</scene>, resolution 2.25Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3enl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3enl OCA], [http://www.ebi.ac.uk/pdbsum/3enl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3enl RCSB]</span> | ||
}} | }} | ||
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[[Category: Lebioda, L.]] | [[Category: Lebioda, L.]] | ||
[[Category: Stec, B.]] | [[Category: Stec, B.]] | ||
| - | [[Category: SO4]] | ||
[[Category: carbon-oxygen lyase]] | [[Category: carbon-oxygen lyase]] | ||
| - | ''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 05:33:09 2008'' |
Revision as of 02:33, 31 March 2008
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| , resolution 2.25Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Phosphopyruvate hydratase, with EC number 4.2.1.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION
Overview
The crystal structure of apo-enolase from baker's yeast (Saccharomyces cerevisiae) was established at 2.25 A resolution using a restrained least-squares refinement method. Based on 21,077 independent reflections of better than 8 A resolution, a final R-factor of 15.4% was obtained with a model obeying standard geometry within 0.017 A in bond length and 3.5 degrees in bond angles. The upper limit for the co-ordinate accuracy of the atoms was estimated to be 0.18 A. The refinement confirmed the heterodox, non-parallel character of the 8-fold beta alpha-barrel domain with beta beta alpha alpha(beta alpha)6 topology. The reported structure for which the data were collected at pH 5.0 represents an apo-form of the enzyme. Of the three carboxylic ligands that form the conformational metal ion binding site two, Glu295 and Asp320, are very close and presumably form a strong acidic type hydrogen bond with the proton partially replacing the electric charge of the physiological cofactor Mg2+. The single sulfate ion found in the structure is in the active site cavity, co-ordinated to the side-chains of Lys345 and Arg374, and to the N atom of Ser375. It is located about 7.4 A from the conformational metal ion binding site. It occupies the site in which the phosphate group of the substrate binds.
About this Structure
3ENL is a Single protein structure of sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entries 2ENL and 1ENL. Full crystallographic information is available from OCA.
Reference
Refined structure of yeast apo-enolase at 2.25 A resolution., Stec B, Lebioda L, J Mol Biol. 1990 Jan 5;211(1):235-48. PMID:2405163
Page seeded by OCA on Mon Mar 31 05:33:09 2008
