1xv5

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{{Seed}}
 
[[Image:1xv5.png|left|200px]]
[[Image:1xv5.png|left|200px]]
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{{STRUCTURE_1xv5| PDB=1xv5 | SCENE= }}
{{STRUCTURE_1xv5| PDB=1xv5 | SCENE= }}
===alpha-glucosyltransferase (AGT) in complex with UDP===
===alpha-glucosyltransferase (AGT) in complex with UDP===
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{{ABSTRACT_PUBMED_16081100}}
{{ABSTRACT_PUBMED_16081100}}
==About this Structure==
==About this Structure==
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1XV5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV5 OCA].
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[[1xv5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV5 OCA].
==Reference==
==Reference==
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Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase., Lariviere L, Sommer N, Morera S, J Mol Biol. 2005 Sep 9;352(1):139-50. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16081100 16081100]
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<ref group="xtra">PMID:016081100</ref><references group="xtra"/>
[[Category: DNA alpha-glucosyltransferase]]
[[Category: DNA alpha-glucosyltransferase]]
[[Category: Enterobacteria phage t4]]
[[Category: Enterobacteria phage t4]]
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[[Category: Single protein]]
 
[[Category: Lariviere, L.]]
[[Category: Lariviere, L.]]
[[Category: Morera, S.]]
[[Category: Morera, S.]]
[[Category: Sommer, N.]]
[[Category: Sommer, N.]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:14:50 2008''
 

Revision as of 13:40, 5 January 2013

Template:STRUCTURE 1xv5

alpha-glucosyltransferase (AGT) in complex with UDP

Template:ABSTRACT PUBMED 16081100

About this Structure

1xv5 is a 1 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA.

Reference

  • Lariviere L, Sommer N, Morera S. Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase. J Mol Biol. 2005 Sep 9;352(1):139-50. PMID:16081100 doi:S0022-2836(05)00784-9

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