2xr0
From Proteopedia
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[[Image:2xr0.png|left|200px]] | [[Image:2xr0.png|left|200px]] | ||
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{{STRUCTURE_2xr0| PDB=2xr0 | SCENE= }} | {{STRUCTURE_2xr0| PDB=2xr0 | SCENE= }} | ||
===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=== | ||
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| - | The line below this paragraph, {{ABSTRACT_PUBMED_21168411}}, adds the Publication Abstract to the page | ||
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{{ABSTRACT_PUBMED_21168411}} | {{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 of [[Beta-lactamase]] 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]. |
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| + | ==See Also== | ||
| + | *[[Beta-lactamase|Beta-lactamase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:021168411</ref><references group="xtra"/> |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: Wang, K K.]] | [[Category: Wang, K K.]] | ||
[[Category: Weiss, K L.]] | [[Category: Weiss, K L.]] | ||
| + | [[Category: Ctx-m-type esbl]] | ||
| + | [[Category: Esbl]] | ||
| + | [[Category: Extended-spectrum beta-lactamase]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 16:56, 26 July 2012
Contents |
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 of Beta-lactamase with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
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
