2pq2: Difference between revisions
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== | ==Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution== | ||
<StructureSection load='2pq2' size='340' side='right'caption='[[2pq2]], [[Resolution|resolution]] 1.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2pq2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PQ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PQ2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=2pq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pq2 OCA], [https://pdbe.org/2pq2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pq2 RCSB], [https://www.ebi.ac.uk/pdbsum/2pq2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pq2 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues. | |||
[[ | == 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/pq/2pq2_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2pq2 ConSurf]. | ||
[ | <div style="clear:both"></div> | ||
==See Also== | |||
*[[Proteinase 3D structures|Proteinase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Parengyodontium album]] | |||
[[Category: Dey S]] | |||
[[Category: Ethayathulla AS]] | |||
[[Category: Kaur P]] | |||
[[Category: Sharma S]] | |||
[[Category: Singh AK]] | |||
[[Category: Singh N]] | |||
[[Category: Singh TP]] | |||
[[Category: Sinha M]] | |||
[[Category: Somvanshi RK]] | |||
[[Category: Srinivasan A]] | |||
Latest revision as of 10:45, 9 October 2024
Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolutionStructure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution
Structural highlights
FunctionPRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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