1gkt: Difference between revisions

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[[Image:1gkt.gif|left|200px]]<br /><applet load="1gkt" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1gkt.gif|left|200px]]
caption="1gkt, resolution 2.1&Aring;" />
 
'''NEUTRON LAUE DIFFRACTION STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH TRANSITION STATE ANALOGUE INHIBITOR H261'''<br />
{{Structure
|PDB= 1gkt |SIZE=350|CAPTION= <scene name='initialview01'>1gkt</scene>, resolution 2.1&Aring;
|SITE= <scene name='pdbsite=CAT:Catalytic'>CAT</scene>
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22]
|GENE=
}}
 
'''NEUTRON LAUE DIFFRACTION STRUCTURE OF ENDOTHIAPEPSIN COMPLEXED WITH TRANSITION STATE ANALOGUE INHIBITOR H261'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1GKT is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Active as [http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] Known structural/functional Site: <scene name='pdbsite=CAT:Catalytic'>CAT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GKT OCA].  
1GKT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GKT OCA].  


==Reference==
==Reference==
A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism., Coates L, Erskine PT, Wood SP, Myles DA, Cooper JB, Biochemistry. 2001 Nov 6;40(44):13149-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11683623 11683623]
A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism., Coates L, Erskine PT, Wood SP, Myles DA, Cooper JB, Biochemistry. 2001 Nov 6;40(44):13149-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11683623 11683623]
[[Category: Cryphonectria parasitica]]
[[Category: Cryphonectria parasitica]]
[[Category: Endothiapepsin]]
[[Category: Endothiapepsin]]
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[[Category: neutron diffraction]]
[[Category: neutron diffraction]]


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