2xr0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{Seed}}
+
[[Image:2xr0.png|left|200px]]
-
[[Image:2xr0.jpg|left|200px]]
+
<!--
<!--
Line 12: Line 11:
===ROOM TEMPERATURE X-RAY STRUCTURE OF THE PERDEUTERATED TOHO-1 R274N R276N DOUBLE MUTANT BETA-LACTAMASE===
===ROOM TEMPERATURE X-RAY STRUCTURE OF THE PERDEUTERATED TOHO-1 R274N R276N DOUBLE MUTANT BETA-LACTAMASE===
 +
 +
<!--
 +
The line below this paragraph, {{ABSTRACT_PUBMED_21168411}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 21168411 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_21168411}}
==About this Structure==
==About this Structure==
-
2XR0 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XR0 OCA].
+
[[2xr0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XR0 OCA].
 +
 
 +
==Reference==
 +
<ref group="xtra">PMID:21168411</ref><references group="xtra"/>
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
Line 28: Line 36:
[[Category: Extended-spectrum beta-lactamase]]
[[Category: Extended-spectrum beta-lactamase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:50:17 2010''
 

Revision as of 18:01, 29 December 2010

Template:STRUCTURE 2xr0

ROOM TEMPERATURE X-RAY STRUCTURE OF THE PERDEUTERATED TOHO-1 R274N R276N DOUBLE MUTANT BETA-LACTAMASE

Template:ABSTRACT PUBMED 21168411

About this Structure

2xr0 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Tomanicek SJ, Wang KK, Weiss KL, Blakeley MP, Cooper J, Chen Y, Coates L. The active site protonation states of perdeuterated Toho-1 beta-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation. FEBS Lett. 2010 Dec 17. PMID:21168411 doi:10.1016/j.febslet.2010.12.017

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools