2vtf

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===X-RAY CRYSTAL STRUCTURE OF THE ENDO-BETA-N-ACETYLGLUCOSAMINIDASE FROM ARTHROBACTER PROTOPHORMIAE E173Q MUTANT REVEALS A TIM BARREL CATALYTIC DOMAIN AND TWO ANCILLARY DOMAINS===
===X-RAY CRYSTAL STRUCTURE OF THE ENDO-BETA-N-ACETYLGLUCOSAMINIDASE FROM ARTHROBACTER PROTOPHORMIAE E173Q MUTANT REVEALS A TIM BARREL CATALYTIC DOMAIN AND TWO ANCILLARY DOMAINS===
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{{ABSTRACT_PUBMED_19327363}}
==About this Structure==
==About this Structure==
2VTF is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Arthrobacter_protophormiae Arthrobacter protophormiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTF OCA].
2VTF is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Arthrobacter_protophormiae Arthrobacter protophormiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VTF OCA].
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==Reference==
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<ref group="xtra">PMID:19327363</ref><references group="xtra"/>
[[Category: Arthrobacter protophormiae]]
[[Category: Arthrobacter protophormiae]]
[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
[[Category: Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 17:09, 8 April 2009

Template:STRUCTURE 2vtf

X-RAY CRYSTAL STRUCTURE OF THE ENDO-BETA-N-ACETYLGLUCOSAMINIDASE FROM ARTHROBACTER PROTOPHORMIAE E173Q MUTANT REVEALS A TIM BARREL CATALYTIC DOMAIN AND TWO ANCILLARY DOMAINS

Template:ABSTRACT PUBMED 19327363

About this Structure

2VTF is a 2 chains structure of sequences from Arthrobacter protophormiae. Full crystallographic information is available from OCA.

Reference

  • Ling Z, Suits MD, Bingham RJ, Bruce NC, Davies GJ, Fairbanks AJ, Moir JW, Taylor EJ. The X-ray crystal structure of an Arthrobacter protophormiae endo-beta-N-acetylglucosaminidase reveals a (beta/alpha)(8) catalytic domain, two ancillary domains and active site residues key for transglycosylation activity. J Mol Biol. 2009 May 29;389(1):1-9. Epub 2009 Mar 24. PMID:19327363 doi:10.1016/j.jmb.2009.03.050

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