4n6n

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==Crystal structure of oxidized legumain in complex with cystatin E/M==
==Crystal structure of oxidized legumain in complex with cystatin E/M==
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<StructureSection load='4n6n' size='340' side='right' caption='[[4n6n]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
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<StructureSection load='4n6n' size='340' side='right'caption='[[4n6n]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4n6n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N6N FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4n6n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N6N FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n6l|4n6l]], [[4n6m|4n6m]], [[4n6o|4n6o]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [https://pdbe.org/4n6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [https://www.ebi.ac.uk/pdbsum/4n6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6n ProSAT]</span></td></tr>
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<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>
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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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [http://www.ebi.ac.uk/pdbsum/4n6n PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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. [[http://www.uniprot.org/uniprot/CYTM_HUMAN CYTM_HUMAN]] Shows moderate inhibition of cathepsin B but is not active against cathepsin C.
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[https://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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 4n6n" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Legumain]]
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[[Category: Homo sapiens]]
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[[Category: Brandstetter, H]]
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[[Category: Large Structures]]
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[[Category: Dall, E]]
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[[Category: Brandstetter H]]
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[[Category: Asparaginyl endopeptidase]]
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[[Category: Dall E]]
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[[Category: Cancer]]
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[[Category: Cathepsin]]
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[[Category: Complex]]
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[[Category: Cysteine protease]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Inhibitor]]
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[[Category: Papain]]
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[[Category: Reactive center loop]]
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Current revision

Crystal structure of oxidized legumain in complex with cystatin E/M

PDB ID 4n6n

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