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{{Seed}}
[[Image:3oea.png|left|200px]]
[[Image:3oea.png|left|200px]]


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{{STRUCTURE_3oea|  PDB=3oea  |  SCENE=  }}  
{{STRUCTURE_3oea|  PDB=3oea  |  SCENE=  }}  


===Crystal structure of the Q121E mutants of C.polysaccharolyticus CBM16-1 bound to cellopentaose===
===Crystal structure of the Q121E mutants of C.polysaccharolyticus CBM16-1 bound to cellopentaose===


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{{ABSTRACT_PUBMED_20739280}}
{{ABSTRACT_PUBMED_20739280}}


==About this Structure==
==About this Structure==
3OEA is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Caldanaerobius_polysaccharolyticus Caldanaerobius polysaccharolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OEA OCA].  
[[3oea]] is a 2 chain structure of [[Glucanase]] with sequence from [http://en.wikipedia.org/wiki/Caldanaerobius_polysaccharolyticus Caldanaerobius polysaccharolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OEA OCA].  
 
==See Also==
*[[Glucanase|Glucanase]]


==Reference==
==Reference==
<ref group="xtra">PMID:20739280</ref><references group="xtra"/>
<ref group="xtra">PMID:020739280</ref><references group="xtra"/>
[[Category: Caldanaerobius polysaccharolyticus]]
[[Category: Caldanaerobius polysaccharolyticus]]
[[Category: Agarwal, V.]]
[[Category: Agarwal, V.]]
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[[Category: Cellopentaose]]
[[Category: Cellopentaose]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 15 08:14:11 2010''

Revision as of 19:47, 26 July 2012

File:3oea.png

Template:STRUCTURE 3oea

Crystal structure of the Q121E mutants of C.polysaccharolyticus CBM16-1 bound to cellopentaose

Template:ABSTRACT PUBMED 20739280

About this Structure

3oea is a 2 chain structure of Glucanase with sequence from Caldanaerobius polysaccharolyticus. Full crystallographic information is available from OCA.

See Also

Reference

  1. Su X, Agarwal V, Dodd D, Bae B, Mackie RI, Nair SK, Cann IK. Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules. J Biol Chem. 2010 Nov 5;285(45):34665-76. Epub 2010 Aug 25. PMID:20739280 doi:10.1074/jbc.M110.168302

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