5lub
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human legumain (AEP) in complex with compound 11== | |
| - | + | <StructureSection load='5lub' size='340' side='right' caption='[[5lub]], [[Resolution|resolution]] 2.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5lub]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LUB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LUB FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3Y7:7-(MORPHOLIN-4-YL)-2,1,3-BENZOXADIAZOL-4-AMINE'>3Y7</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Legumain Legumain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.34 3.4.22.34] </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=5lub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lub OCA], [http://pdbe.org/5lub PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lub RCSB], [http://www.ebi.ac.uk/pdbsum/5lub PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lub ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/LGMN_HUMAN LGMN_HUMAN]] Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Legumain]] | ||
| + | [[Category: Brandstetter, H]] | ||
| + | [[Category: Dall, E]] | ||
| + | [[Category: Ye, K]] | ||
| + | [[Category: Allosteric inhibitor]] | ||
| + | [[Category: Alzheimer's disease]] | ||
| + | [[Category: Asparaginyl endopeptidase]] | ||
| + | [[Category: Cysteine protease]] | ||
| + | [[Category: Hydrolase]] | ||
Revision as of 13:46, 29 March 2017
Crystal structure of human legumain (AEP) in complex with compound 11
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