2qin: Difference between revisions
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[[Image:2qin.png|left|200px]] | [[Image:2qin.png|left|200px]] | ||
{{STRUCTURE_2qin| PDB=2qin | SCENE= }} | {{STRUCTURE_2qin| PDB=2qin | SCENE= }} | ||
===Stenotrophomonas maltophilia L1 Metallo-beta-Lactamase Asp-120 Cys mutant=== | ===Stenotrophomonas maltophilia L1 Metallo-beta-Lactamase Asp-120 Cys mutant=== | ||
{{ABSTRACT_PUBMED_17715946}} | {{ABSTRACT_PUBMED_17715946}} | ||
==About this Structure== | ==About this Structure== | ||
[[2qin]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIN OCA]. | [[2qin]] is a 4 chain structure of [[Beta-lactamase]] with sequence from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QIN OCA]. | ||
==See Also== | |||
*[[Beta-lactamase|Beta-lactamase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:017715946</ref><ref group="xtra">PMID:014573595</ref><references group="xtra"/> | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Stenotrophomonas maltophilia]] | [[Category: Stenotrophomonas maltophilia]] | ||
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[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Metallo-beta-lactamase]] | [[Category: Metallo-beta-lactamase]] | ||
Revision as of 20:03, 25 July 2012
Stenotrophomonas maltophilia L1 Metallo-beta-Lactamase Asp-120 Cys mutantStenotrophomonas maltophilia L1 Metallo-beta-Lactamase Asp-120 Cys mutant
Template:ABSTRACT PUBMED 17715946
About this StructureAbout this Structure
2qin is a 4 chain structure of Beta-lactamase with sequence from Stenotrophomonas maltophilia. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Crisp J, Conners R, Garrity JD, Carenbauer AL, Crowder MW, Spencer J. Structural basis for the role of Asp-120 in metallo-beta-lactamases. Biochemistry. 2007 Sep 18;46(37):10664-74. Epub 2007 Aug 23. PMID:17715946 doi:10.1021/bi700707u
- ↑ Garrity JD, Carenbauer AL, Herron LR, Crowder MW. Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis. J Biol Chem. 2004 Jan 9;279(2):920-7. Epub 2003 Oct 22. PMID:14573595 doi:10.1074/jbc.M309852200