3i37
From Proteopedia
(Difference between revisions)
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<StructureSection load='3i37' size='340' side='right'caption='[[3i37]], [[Resolution|resolution]] 0.99Å' scene=''> | <StructureSection load='3i37' size='340' side='right'caption='[[3i37]], [[Resolution|resolution]] 0.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3i37]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3i37]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tritirachium_album Tritirachium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3I37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I37 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></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></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i2y|3i2y]], [[3i30|3i30]], [[3i34|3i34]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3i2y|3i2y]], [[3i30|3i30]], [[3i34|3i34]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [https://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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3i37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i37 OCA], [https://pdbe.org/3i37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i37 RCSB], [https://www.ebi.ac.uk/pdbsum/3i37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i37 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] Hydrolyzes keratin at aromatic and hydrophobic residues. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Proteinase|Proteinase]] | ||
*[[Proteinase 3D structures|Proteinase 3D structures]] | *[[Proteinase 3D structures|Proteinase 3D structures]] | ||
__TOC__ | __TOC__ | ||
Revision as of 11:21, 6 April 2022
Proteinase K by LB Nanotemplate Method before high X-Ray dose on ID14-2 Beamline at ESRF
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