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2pyz
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2pyz]] is a 1 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=2PYZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PYZ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2pyz]] is a 1 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=2PYZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PYZ FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU4:4,4-(AMINOMETHYLENE)BIS(N,N-DIMETHYLANILINE)'>AU4</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU4:4,4-(AMINOMETHYLENE)BIS(N,N-DIMETHYLANILINE)'>AU4</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pwb|2pwb]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pwb|2pwb]]</td></tr> |
| - | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pyz RCSB], [http://www.ebi.ac.uk/pdbsum/2pyz 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=2pyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2pyz RCSB], [http://www.ebi.ac.uk/pdbsum/2pyz PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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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[[Category: Engyodontium album]] | [[Category: Engyodontium album]] | ||
[[Category: Peptidase K]] | [[Category: Peptidase K]] | ||
| - | [[Category: Bhushan, A | + | [[Category: Bhushan, A]] |
| - | [[Category: Kaur, P | + | [[Category: Kaur, P]] |
| - | [[Category: Sharma, S | + | [[Category: Sharma, S]] |
| - | [[Category: Singh, A K | + | [[Category: Singh, A K]] |
| - | [[Category: Singh, N | + | [[Category: Singh, N]] |
| - | [[Category: Singh, T P | + | [[Category: Singh, T P]] |
| - | [[Category: Sinha, M | + | [[Category: Sinha, M]] |
[[Category: Enzyme activity]] | [[Category: Enzyme activity]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Inhibition]] | [[Category: Inhibition]] | ||
Revision as of 04:23, 25 December 2014
Crystal structure of the complex of proteinase K with auramine at 1.8A resolution
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Categories: Engyodontium album | Peptidase K | Bhushan, A | Kaur, P | Sharma, S | Singh, A K | Singh, N | Singh, T P | Sinha, M | Enzyme activity | Hydrolase | Inhibition
