2frq: Difference between revisions

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[[Image:2frq.png|left|200px]]


{{STRUCTURE_2frq|  PDB=2frq  |  SCENE=  }}
==Human Cathepsin S with Inhibitor CRA-26871==
 
<StructureSection load='2frq' size='340' side='right'caption='[[2frq]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
===Human Cathepsin S with Inhibitor CRA-26871===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[2frq]] 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=2FRQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FRQ FirstGlance]. <br>
 
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C71:N-[4-(AMINOMETHYL)-1,1-DIOXIDOTETRAHYDRO-2H-THIOPYRAN-4-YL]-3-(1-METHYLCYCLOPENTYL)-N~2~-[(1E)-N-(PHENYLSULFONYL)ETHANIMIDOYL]-L-ALANINAMIDE'>C71</scene></td></tr>
==About this Structure==
<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>
[[2frq]] is a 2 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=2FRQ OCA].  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2frq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2frq OCA], [https://pdbe.org/2frq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2frq RCSB], [https://www.ebi.ac.uk/pdbsum/2frq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2frq ProSAT]</span></td></tr>
</table>
== Function ==
[[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fr/2frq_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2frq ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Cathepsin|Cathepsin]]
*[[Cathepsin 3D structures|Cathepsin 3D structures]]
__TOC__
</StructureSection>
[[Category: Cathepsin S]]
[[Category: Cathepsin S]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Somoza, J R.]]
[[Category: Large Structures]]
[[Category: 26871]]
[[Category: Somoza, J R]]
[[Category: Cysteine protease]]
[[Category: Cysteine protease]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Papain]]
[[Category: Papain]]
[[Category: Proteinase]]
[[Category: Proteinase]]

Latest revision as of 12:56, 5 May 2021

Human Cathepsin S with Inhibitor CRA-26871Human Cathepsin S with Inhibitor CRA-26871

Structural highlights

2frq is a 2 chain structure with sequence from Human. 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, PDBe, RCSB, PDBsum, ProSAT

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

2frq, resolution 1.60Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA