2pq2: Difference between revisions
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==Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution== | ==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=''> | <StructureSection load='2pq2' size='340' side='right' caption='[[2pq2]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dp4|2dp4]], [[2dqk|2dqk]], [[2duj|2duj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dp4|2dp4]], [[2dqk|2dqk]], [[2duj|2duj]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </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=2pq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pq2 OCA], [http://pdbe.org/2pq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pq2 RCSB], [http://www.ebi.ac.uk/pdbsum/2pq2 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=2pq2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pq2 OCA], [http://pdbe.org/2pq2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pq2 RCSB], [http://www.ebi.ac.uk/pdbsum/2pq2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pq2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pq/2pq2_consurf.spt"</scriptWhenChecked> | <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/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 11:15, 29 August 2018
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
Function[PRTK_TRIAL] 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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