We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
2xr0
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | [[Image:2xr0.png|left|200px]] | |
| - | [[Image:2xr0. | + | |
<!-- | <!-- | ||
| 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]. | |
| + | |||
| + | ==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
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
