This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3enl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:3enl.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3enl.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3enl| PDB=3enl | SCENE= }}
{{STRUCTURE_3enl| PDB=3enl | SCENE= }}
-
'''REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_2405163}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 2405163 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_2405163}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Stec, B.]]
[[Category: Stec, B.]]
[[Category: Carbon-oxygen lyase]]
[[Category: Carbon-oxygen lyase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:00:49 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:28:25 2008''

Revision as of 03:28, 29 July 2008

Image:3enl.png

Template:STRUCTURE 3enl

REFINED STRUCTURE OF YEAST APO-ENOLASE AT 2.25 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 2405163

About this Structure

3ENL is a Single protein structure of sequence from Saccharomyces cerevisiae. This structure supersedes the now removed PDB entries 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 Tue Jul 29 06:28:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3enl"
Personal tools