2hh5

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<StructureSection load='2hh5' size='340' side='right'caption='[[2hh5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='2hh5' size='340' side='right'caption='[[2hh5]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2hh5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HH5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2hh5]] 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=2HH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HH5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GNQ:N-[(1R)-1-[(BENZYLSULFONYL)METHYL]-2-{[(1S)-1-METHYL-2-{[4-(TRIFLUOROMETHOXY)PHENYL]AMINO}ETHYL]AMINO}-2-OXOETHYL]MORPHOLINE-4-CARBOXAMIDE'>GNQ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2f1g|2f1g]], [[2hhn|2hhn]]</div></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GNQ:N-[(1R)-1-[(BENZYLSULFONYL)METHYL]-2-{[(1S)-1-METHYL-2-{[4-(TRIFLUOROMETHOXY)PHENYL]AMINO}ETHYL]AMINO}-2-OXOETHYL]MORPHOLINE-4-CARBOXAMIDE'>GNQ</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTSS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></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=2hh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hh5 OCA], [https://pdbe.org/2hh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hh5 RCSB], [https://www.ebi.ac.uk/pdbsum/2hh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hh5 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=2hh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hh5 OCA], [https://pdbe.org/2hh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hh5 RCSB], [https://www.ebi.ac.uk/pdbsum/2hh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hh5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN]] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
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[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cathepsin S]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Harris, J L]]
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[[Category: Harris JL]]
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[[Category: Hornsby, M]]
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[[Category: Hornsby M]]
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[[Category: Karenewsky, D S]]
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[[Category: Karenewsky DS]]
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[[Category: Lesley, S A]]
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[[Category: Lesley SA]]
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[[Category: Spraggon, G]]
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[[Category: Spraggon G]]
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[[Category: Tully, D C]]
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[[Category: Tully DC]]
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[[Category: Arylaminoethyl-amide]]
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[[Category: Cathepsin s]]
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[[Category: Hydrolase]]
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[[Category: Inhibition]]
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[[Category: Noncovalent]]
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[[Category: Zinc]]
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Revision as of 09:57, 30 August 2023

Crystal Structure of Cathepsin S in complex with a Zinc mediated non-covalent arylaminoethyl amide

PDB ID 2hh5

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