5p6r

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m (Protected "5p6r" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5p6r is ON HOLD
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==Automated refinement of diffraction data obtained from an endothiapepsin crystal treated with fragment 288==
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<StructureSection load='5p6r' size='340' side='right' caption='[[5p6r]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
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Authors: Schiebel, J., Heine, A., Klebe, G.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5p6r]] is a 1 chain structure with sequence 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=5P6R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5P6R FirstGlance]. <br>
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Description: Automated refinement of diffraction data obtained from an endothiapepsin crystal treated with fragment 288
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5p6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5p6r OCA], [http://pdbe.org/5p6r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5p6r RCSB], [http://www.ebi.ac.uk/pdbsum/5p6r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5p6r ProSAT]</span></td></tr>
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</table>
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__TOC__
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</StructureSection>
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[[Category: Cryphonectria parasitica]]
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[[Category: Endothiapepsin]]
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[[Category: Heine, A]]
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[[Category: Klebe, G]]
[[Category: Schiebel, J]]
[[Category: Schiebel, J]]
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[[Category: Klebe, G]]
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[[Category: Aspartic protease]]
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[[Category: Heine, A]]
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[[Category: Fragment screening]]
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[[Category: Hydrolase]]
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[[Category: Method development]]

Revision as of 04:39, 4 August 2016

Automated refinement of diffraction data obtained from an endothiapepsin crystal treated with fragment 288

5p6r, resolution 1.27Å

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