1fbw: Difference between revisions

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[[Image:1fbw.jpg|left|200px]]<br /><applet load="1fbw" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1fbw.jpg|left|200px]]
caption="1fbw, resolution 2.0&Aring;" />
 
'''Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellohexaose'''<br />
{{Structure
|PDB= 1fbw |SIZE=350|CAPTION= <scene name='initialview01'>1fbw</scene>, resolution 2.0&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]
|GENE=
}}
 
'''Crystal structure of the cellulase CEL48F from C. cellulolyticum in complex with cellohexaose'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1FBW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBW OCA].  
1FBW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_cellulolyticum Clostridium cellulolyticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FBW OCA].  


==Reference==
==Reference==
Crystal structures of the cellulase Cel48F in complex with inhibitors and substrates give insights into its processive action., Parsiegla G, Reverbel-Leroy C, Tardif C, Belaich JP, Driguez H, Haser R, Biochemistry. 2000 Sep 19;39(37):11238-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10985769 10985769]
Crystal structures of the cellulase Cel48F in complex with inhibitors and substrates give insights into its processive action., Parsiegla G, Reverbel-Leroy C, Tardif C, Belaich JP, Driguez H, Haser R, Biochemistry. 2000 Sep 19;39(37):11238-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10985769 10985769]
[[Category: Cellulase]]
[[Category: Cellulase]]
[[Category: Clostridium cellulolyticum]]
[[Category: Clostridium cellulolyticum]]
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[[Category: protein-cellohexaose complex]]
[[Category: protein-cellohexaose complex]]


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