1xv5: Difference between revisions

No edit summary
No edit summary
Line 1: Line 1:
[[Image:1xv5.gif|left|200px]]<br /><applet load="1xv5" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1xv5.gif|left|200px]]
caption="1xv5, resolution 1.73&Aring;" />
 
'''alpha-glucosyltransferase (AGT) in complex with UDP'''<br />
{{Structure
|PDB= 1xv5 |SIZE=350|CAPTION= <scene name='initialview01'>1xv5</scene>, resolution 1.73&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=UDP:URIDINE-5'-DIPHOSPHATE'>UDP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/DNA_alpha-glucosyltransferase DNA alpha-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.26 2.4.1.26]
|GENE=
}}
 
'''alpha-glucosyltransferase (AGT) in complex with UDP'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
1XV5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=UDP:'>UDP</scene>, <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA_alpha-glucosyltransferase DNA alpha-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.26 2.4.1.26] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV5 OCA].  
1XV5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t4 Bacteriophage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XV5 OCA].  


==Reference==
==Reference==
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16081100 16081100]
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]
[[Category: Bacteriophage t4]]
[[Category: Bacteriophage t4]]
[[Category: DNA alpha-glucosyltransferase]]
[[Category: DNA alpha-glucosyltransferase]]
Line 23: Line 32:
[[Category: transferase]]
[[Category: transferase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:58:56 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:14:54 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA