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| | <StructureSection load='5p4e' size='340' side='right'caption='[[5p4e]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='5p4e' size='340' side='right'caption='[[5p4e]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5p4e]] 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=5P4E OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5P4E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5p4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5P4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5P4E FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.399Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5p4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5p4e OCA], [http://pdbe.org/5p4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5p4e RCSB], [http://www.ebi.ac.uk/pdbsum/5p4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5p4e ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5p4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5p4e OCA], [https://pdbe.org/5p4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5p4e RCSB], [https://www.ebi.ac.uk/pdbsum/5p4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5p4e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CARP_CRYPA CARP_CRYPA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5p4e" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5p4e" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Pepsin|Pepsin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Cryphonectria parasitica]] | | [[Category: Cryphonectria parasitica]] |
| - | [[Category: Endothiapepsin]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Heine, A]] | + | [[Category: Heine A]] |
| - | [[Category: Klebe, G]] | + | [[Category: Klebe G]] |
| - | [[Category: Schiebel, J]] | + | [[Category: Schiebel J]] |
| - | [[Category: Aspartic protease]]
| + | |
| - | [[Category: Fragment screening]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Method development]]
| + | |
| Structural highlights
Function
CARP_CRYPA
Publication Abstract from PubMed
Today the identification of lead structures for drug development often starts from small fragment-like molecules raising the chances to find compounds that successfully pass clinical trials. At the heart of the screening for fragments binding to a specific target, crystallography delivers structural information essential for subsequent drug design. While it is common to search for bound ligands in electron densities calculated directly after an initial refinement cycle, we raise the important question whether this strategy is viable for fragments characterized by low affinities. Here, we describe and provide a collection of high-quality diffraction data obtained from 364 protein crystals treated with diverse fragments. Subsequent data analysis showed that approximately 25% of all hits would have been missed without further refining the resulting structures. To enable fast and reliable hit identification, we have designed an automated refinement pipeline that will inspire the development of optimized tools facilitating the successful application of fragment-based methods.
High-Throughput Crystallography: Reliable and Efficient Identification of Fragment Hits.,Schiebel J, Krimmer SG, Rower K, Knorlein A, Wang X, Park AY, Stieler M, Ehrmann FR, Fu K, Radeva N, Krug M, Huschmann FU, Glockner S, Weiss MS, Mueller U, Klebe G, Heine A Structure. 2016 Aug 2;24(8):1398-409. doi: 10.1016/j.str.2016.06.010. Epub 2016, Jul 21. PMID:27452405[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schiebel J, Krimmer SG, Rower K, Knorlein A, Wang X, Park AY, Stieler M, Ehrmann FR, Fu K, Radeva N, Krug M, Huschmann FU, Glockner S, Weiss MS, Mueller U, Klebe G, Heine A. High-Throughput Crystallography: Reliable and Efficient Identification of Fragment Hits. Structure. 2016 Aug 2;24(8):1398-409. doi: 10.1016/j.str.2016.06.010. Epub 2016, Jul 21. PMID:27452405 doi:http://dx.doi.org/10.1016/j.str.2016.06.010
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