1k17: Difference between revisions

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{{Theoretical_model}}
{{Theoretical_model}}
{{Seed}}
 
[[Image:1k17.png|left|200px]]
[[Image:1k17.png|left|200px]]


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{{STRUCTURE_1k17|  PDB=1k17  |  SCENE=  }}  
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===ALIPHATIC AMIDASE (EC 3.5.1.4)===
===ALIPHATIC AMIDASE (EC 3.5.1.4)===


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{{ABSTRACT_PUBMED_11955282}}
{{ABSTRACT_PUBMED_11955282}}
==About this Structure==
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K17 OCA].


==Reference==
==Reference==
<ref group="xtra">PMID:11955282</ref><references group="xtra"/>
<ref group="xtra">PMID:011955282</ref><references group="xtra"/>
[[Category: Brown, P R]]
[[Category: Brown, P R]]
[[Category: Clemente, A]]
[[Category: Clemente, A]]
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[[Category: Novo, C]]
[[Category: Novo, C]]
[[Category: Tata, R]]
[[Category: Tata, R]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr  8 06:59:52 2010''

Revision as of 11:48, 21 October 2012

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.
File:1k17.png

Template:STRUCTURE 1k17

ALIPHATIC AMIDASE (EC 3.5.1.4)ALIPHATIC AMIDASE (EC 3.5.1.4)

Template:ABSTRACT PUBMED 11955282

ReferenceReference

[xtra 1]

  1. Novo C, Farnaud S, Tata R, Clemente A, Brown PR. Support for a three-dimensional structure predicting a Cys-Glu-Lys catalytic triad for Pseudomonas aeruginosa amidase comes from site-directed mutagenesis and mutations altering substrate specificity. Biochem J. 2002 Aug 1;365(Pt 3):731-8. PMID:11955282 doi:10.1042/BJ20011714

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