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=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pq2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium 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 [http:// | <table><tr><td colspan='2'>[[2pq2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium 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 [http://proteopedia.org/fgij/fg.htm?mol=2PQ2 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> | </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='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:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/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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==See Also== | ==See Also== | ||
*[[Proteinase|Proteinase]] | *[[Proteinase|Proteinase]] | ||
*[[Proteinase 3D structures|Proteinase 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Engyodontium album]] | [[Category: Engyodontium album]] | ||
[[Category: Large Structures]] | |||
[[Category: Peptidase K]] | [[Category: Peptidase K]] | ||
[[Category: Dey, S]] | [[Category: Dey, S]] | ||
Revision as of 09:57, 3 June 2020
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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