1ko3
From Proteopedia
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[[Image:1ko3.png|left|200px]] | [[Image:1ko3.png|left|200px]] | ||
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{{STRUCTURE_1ko3| PDB=1ko3 | SCENE= }} | {{STRUCTURE_1ko3| PDB=1ko3 | SCENE= }} | ||
===VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced=== | ===VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced=== | ||
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==About this Structure== | ==About this Structure== | ||
- | + | [[1ko3]] is a 1 chain structure of [[Beta-lactamase]] with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KO3 OCA]. | |
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+ | ==See Also== | ||
+ | *[[Beta-lactamase|Beta-lactamase]] | ||
==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:018061205</ref><ref group="xtra">PMID:015779910</ref><ref group="xtra">PMID:018052313</ref><references group="xtra"/> |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
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[[Category: Alpha-beta/beta-alpha fold]] | [[Category: Alpha-beta/beta-alpha fold]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
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Revision as of 20:07, 25 July 2012
Contents |
VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced
Template:ABSTRACT PUBMED 18061205
About this Structure
1ko3 is a 1 chain structure of Beta-lactamase with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
See Also
Reference
- Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O. The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form. J Mol Biol. 2008 Jan 18;375(3):604-11. Epub 2007 Nov 13. PMID:18061205 doi:10.1016/j.jmb.2007.11.012
- Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM. Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism. Biochemistry. 2005 Mar 29;44(12):4841-9. PMID:15779910 doi:10.1021/bi047709t
- Yamaguchi Y, Jin W, Matsunaga K, Ikemizu S, Yamagata Y, Wachino J, Shibata N, Arakawa Y, Kurosaki H. Crystallographic investigation of the inhibition mode of a VIM-2 metallo-beta-lactamase from Pseudomonas aeruginosa by a mercaptocarboxylate inhibitor. J Med Chem. 2007 Dec 27;50(26):6647-53. Epub 2007 Dec 6. PMID:18052313 doi:10.1021/jm701031n