2d2o: Difference between revisions

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[[Image:2d2o.gif|left|200px]]<br /><applet load="2d2o" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2d2o.gif|left|200px]]
caption="2d2o, resolution 2.10&Aring;" />
 
'''Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft'''<br />
{{Structure
|PDB= 2d2o |SIZE=350|CAPTION= <scene name='initialview01'>2d2o</scene>, resolution 2.10&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135]
|GENE=
}}
 
'''Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2D2O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2O OCA].  
2D2O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2O OCA].  


==Reference==
==Reference==
Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft., Ohtaki A, Mizuno M, Yoshida H, Tonozuka T, Sakano Y, Kamitori S, Carbohydr Res. 2006 Jun 12;341(8):1041-6. Epub 2006 Mar 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16564038 16564038]
Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft., Ohtaki A, Mizuno M, Yoshida H, Tonozuka T, Sakano Y, Kamitori S, Carbohydr Res. 2006 Jun 12;341(8):1041-6. Epub 2006 Mar 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16564038 16564038]
[[Category: Neopullulanase]]
[[Category: Neopullulanase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: beta/alpha barrel]]
[[Category: beta/alpha barrel]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:48 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:22:34 2008''
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