2fye: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2fye]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FYE FirstGlance]. <br>
<table><tr><td colspan='2'>[[2fye]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FYE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FYE FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCQ:N-[(1R)-1-[({[(5S)-3,5-DIMETHYL-2,5-DIHYDROISOXAZOL-4-YL]METHYL}SULFONYL)METHYL]-2-OXO-2-({(1S)-3-PHENYL-1-[2-(PHENYLSULFONYL)ETHYL]PROPYL}AMINO)ETHYL]MORPHOLINE-4-CARBOXAMIDE'>BCQ</scene><br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCQ:N-[(1R)-1-[({[(5S)-3,5-DIMETHYL-2,5-DIHYDROISOXAZOL-4-YL]METHYL}SULFONYL)METHYL]-2-OXO-2-({(1S)-3-PHENYL-1-[2-(PHENYLSULFONYL)ETHYL]PROPYL}AMINO)ETHYL]MORPHOLINE-4-CARBOXAMIDE'>BCQ</scene></td></tr>
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fye OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fye RCSB], [http://www.ebi.ac.uk/pdbsum/2fye 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=2fye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fye OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2fye RCSB], [http://www.ebi.ac.uk/pdbsum/2fye PDBsum]</span></td></tr>
<table>
</table>
== Function ==
[[http://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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[[Category: Cathepsin S]]
[[Category: Cathepsin S]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Somoza, J R.]]
[[Category: Somoza, J R]]
[[Category: 14013]]
[[Category: Cysteine protease]]
[[Category: Cysteine protease]]
[[Category: Drug design]]
[[Category: Drug design]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Papain]]
[[Category: Papain]]

Revision as of 02:21, 25 December 2014

Mutant Human Cathepsin S with irreversible inhibitor CRA-14013Mutant Human Cathepsin S with irreversible inhibitor CRA-14013

Structural highlights

2fye is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Cathepsin S, with EC number 3.4.22.27
Resources:FirstGlance, OCA, RCSB, PDBsum

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

2fye, resolution 2.20Å

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