2fud: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 2: | Line 2: | ||
<StructureSection load='2fud' size='340' side='right' caption='[[2fud]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='2fud' size='340' side='right' caption='[[2fud]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fud]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2fud]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FUD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FUD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRL:N-{(1R)-2-[(4-CYANO-1,1-DIOXIDOTETRAHYDRO-2H-THIOPYRAN-4-YL)AMINO]-2-OXO-1-[(TRIMETHYLSILYL)METHYL]ETHYL}MORPHOLINE-4-CARBOXAMIDE'>CRL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRL:N-{(1R)-2-[(4-CYANO-1,1-DIOXIDOTETRAHYDRO-2H-THIOPYRAN-4-YL)AMINO]-2-OXO-1-[(TRIMETHYLSILYL)METHYL]ETHYL}MORPHOLINE-4-CARBOXAMIDE'>CRL</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </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=2fud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fud OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fud RCSB], [http://www.ebi.ac.uk/pdbsum/2fud PDBsum]</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=2fud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fud OCA], [http://pdbe.org/2fud PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fud RCSB], [http://www.ebi.ac.uk/pdbsum/2fud PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 25: | Line 25: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cathepsin S]] | [[Category: Cathepsin S]] | ||
[[Category: | [[Category: Human]] | ||
[[Category: Somoza, J R]] | [[Category: Somoza, J R]] | ||
[[Category: Cysteine protease]] | [[Category: Cysteine protease]] | ||
Revision as of 17:59, 10 September 2015
Human Cathepsin S with Inhibitor CRA-27566Human Cathepsin S with Inhibitor CRA-27566
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
| ||||||||||||||||||