3bls

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==About this Structure==
==About this Structure==
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3BLS is a [[Single protein]] structure of 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=3BLS OCA].
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3BLS is a 2 chains structure of sequences 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=3BLS OCA].
==Reference==
==Reference==
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Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design., Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ, Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9819201 9819201]
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<ref group="xtra">PMID:9819201</ref><references group="xtra"/>
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
 
[[Category: Remington, S J.]]
[[Category: Remington, S J.]]
[[Category: Shoichet, B K.]]
[[Category: Shoichet, B K.]]
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[[Category: Serine hydrolase]]
[[Category: Serine hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:30:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:45:13 2009''

Revision as of 14:45, 17 February 2009

Template:STRUCTURE 3bls

AMPC BETA-LACTAMASE FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 9819201

About this Structure

3BLS is a 2 chains structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

  • Usher KC, Blaszczak LC, Weston GS, Shoichet BK, Remington SJ. Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design. Biochemistry. 1998 Nov 17;37(46):16082-92. PMID:9819201 doi:10.1021/bi981210f

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