5ux4
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Rat Cathepsin D with (5S)-3-(5,6-dihydro-2H-pyran-3-yl)-1-fluoro- 7-(2-fluoropyridin-3-yl)spiro[chromeno[2,3- c]pyridine-5,4'-[1,3]oxazol]-2'-amine== | |
| - | + | <StructureSection load='5ux4' size='340' side='right' caption='[[5ux4]], [[Resolution|resolution]] 2.81Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5ux4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UX4 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3UT:(5S)-3-(5,6-DIHYDRO-2H-PYRAN-3-YL)-1-FLUORO-7-(2-FLUOROPYRIDIN-3-YL)SPIRO[CHROMENO[2,3-C]PYRIDINE-5,4-[1,3]OXAZOL]-2-AMINE'>3UT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_D Cathepsin D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.5 3.4.23.5] </span></td></tr> |
| + | <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=5ux4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ux4 OCA], [http://pdbe.org/5ux4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ux4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ux4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ux4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CATD_RAT CATD_RAT]] Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation.[UniProtKB:P07339] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cathepsin D]] | ||
[[Category: Sickmier, A]] | [[Category: Sickmier, A]] | ||
| + | [[Category: Bace1]] | ||
| + | [[Category: Beta amyloid cleaving enzyme]] | ||
| + | [[Category: Cathepsin d]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 07:31, 14 June 2018
Crystal Structure of Rat Cathepsin D with (5S)-3-(5,6-dihydro-2H-pyran-3-yl)-1-fluoro- 7-(2-fluoropyridin-3-yl)spiro[chromeno[2,3- c]pyridine-5,4'-[1,3]oxazol]-2'-amine
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