3a4w

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[[Image:3a4w.png|left|200px]]
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{{STRUCTURE_3a4w| PDB=3a4w | SCENE= }}
{{STRUCTURE_3a4w| PDB=3a4w | SCENE= }}
===Crystal structures of catalytic site mutants of active domain 2 of thermostable chitinase from Pyrococcus furiosus complexed with chito-oligosaccharides===
===Crystal structures of catalytic site mutants of active domain 2 of thermostable chitinase from Pyrococcus furiosus complexed with chito-oligosaccharides===
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{{ABSTRACT_PUBMED_20553502}}
{{ABSTRACT_PUBMED_20553502}}
==About this Structure==
==About this Structure==
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[[3a4w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A4W OCA].
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[[3a4w]] is a 2 chain structure of [[Chitinase]] with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A4W OCA].
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==See Also==
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*[[Chitinase|Chitinase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:20553502</ref><references group="xtra"/>
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<ref group="xtra">PMID:020553502</ref><references group="xtra"/>
[[Category: Chitinase]]
[[Category: Chitinase]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]

Revision as of 19:45, 26 July 2012

Template:STRUCTURE 3a4w

Contents

Crystal structures of catalytic site mutants of active domain 2 of thermostable chitinase from Pyrococcus furiosus complexed with chito-oligosaccharides

Template:ABSTRACT PUBMED 20553502

About this Structure

3a4w is a 2 chain structure of Chitinase with sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

See Also

Reference

  • Tsuji H, Nishimura S, Inui T, Kado Y, Ishikawa K, Nakamura T, Uegaki K. Kinetic and crystallographic analyses of the catalytic domain of chitinase from Pyrococcus furiosus- the role of conserved residues in the active site. FEBS J. 2010 Jun;277(12):2683-95. PMID:20553502 doi:10.1111/j.1742-464X.2010.07685.x

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