2vtf
From Proteopedia
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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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+ | (as it appears on PubMed at http://www.pubmed.gov), where 19327363 is the PubMed ID number. | ||
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==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== | ||
+ | <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
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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