2hp6: Difference between revisions

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[[Image:2hp6.png|left|200px]]
[[Image:2hp6.png|left|200px]]


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{{STRUCTURE_2hp6|  PDB=2hp6  |  SCENE=  }}  
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===Crystal structure of the OXA-10 W154A mutant at pH 7.5===
===Crystal structure of the OXA-10 W154A mutant at pH 7.5===


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{{ABSTRACT_PUBMED_19860471}}


==About this Structure==
==About this Structure==
2HP6 is a 2 chains structure with sequences 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=2HP6 OCA].  
[[2hp6]] is a 2 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=2HP6 OCA].  
 
==See Also==
*[[Beta-lactamase|Beta-lactamase]]


==Reference==
==Reference==
<ref group="xtra">PMID:19860471</ref><references group="xtra"/>
<ref group="xtra">PMID:019860471</ref><references group="xtra"/>
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Lysine carboxylation]]
[[Category: Lysine carboxylation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Aug 12 00:02:17 2010''

Revision as of 18:34, 25 July 2012

File:2hp6.png

Template:STRUCTURE 2hp6

Crystal structure of the OXA-10 W154A mutant at pH 7.5Crystal structure of the OXA-10 W154A mutant at pH 7.5

Template:ABSTRACT PUBMED 19860471

About this StructureAbout this Structure

2hp6 is a 2 chain structure of Beta-lactamase with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. Baurin S, Vercheval L, Bouillenne F, Falzone C, Brans A, Jacquamet L, Ferrer JL, Sauvage E, Dehareng D, Frere JM, Charlier P, Galleni M, Kerff F. Critical role of Tryptophan 154 for the activity and stability of class D beta-lactamases. Biochemistry. 2009 Oct 27. PMID:19860471 doi:10.1021/bi901548c

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