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2zma

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[[Image:2zma.png|left|200px]]
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{{STRUCTURE_2zma| PDB=2zma | SCENE= }}
{{STRUCTURE_2zma| PDB=2zma | SCENE= }}
===Crystal Structure of 6-Aminohexanoate-dimer Hydrolase S112A/G181D/H266N/D370Y Mutant with Substrate===
===Crystal Structure of 6-Aminohexanoate-dimer Hydrolase S112A/G181D/H266N/D370Y Mutant with Substrate===
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{{ABSTRACT_PUBMED_19476493}}
{{ABSTRACT_PUBMED_19476493}}
==About this Structure==
==About this Structure==
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2ZMA is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Flavobacterium_sp. Flavobacterium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZMA OCA].
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[[2zma]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Flavobacterium_sp. Flavobacterium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZMA OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:19476493</ref><references group="xtra"/>
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<ref group="xtra">PMID:019476493</ref><references group="xtra"/>
[[Category: 6-aminohexanoate-dimer hydrolase]]
[[Category: 6-aminohexanoate-dimer hydrolase]]
[[Category: Flavobacterium sp.]]
[[Category: Flavobacterium sp.]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Nylon degradation]]
[[Category: Nylon degradation]]
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[[Category: Plasmid]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 25 08:23:32 2009''
 

Revision as of 18:28, 7 January 2013

Template:STRUCTURE 2zma

Crystal Structure of 6-Aminohexanoate-dimer Hydrolase S112A/G181D/H266N/D370Y Mutant with Substrate

Template:ABSTRACT PUBMED 19476493

About this Structure

2zma is a 1 chain structure with sequence from Flavobacterium sp.. Full crystallographic information is available from OCA.

Reference

  • Kawashima Y, Ohki T, Shibata N, Higuchi Y, Wakitani Y, Matsuura Y, Nakata Y, Takeo M, Kato D, Negoro S. Molecular design of a nylon-6 byproduct-degrading enzyme from a carboxylesterase with a beta-lactamase fold. FEBS J. 2009 May;276(9):2547-56. Epub 2009 Mar 18. PMID:19476493 doi:10.1111/j.1742-4658.2009.06978.x

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