2dqk: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dqk]] 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=2DQK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DQK FirstGlance]. <br> | <table><tr><td colspan='2'>[[2dqk]] 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=2DQK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DQK FirstGlance]. <br> | ||
</td></tr><tr><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><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> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bjr|1bjr]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bjr|1bjr]]</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=2dqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dqk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dqk RCSB], [http://www.ebi.ac.uk/pdbsum/2dqk 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=2dqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dqk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2dqk RCSB], [http://www.ebi.ac.uk/pdbsum/2dqk 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: Dey, S | [[Category: Dey, S]] | ||
[[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: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Proteinsase k]] | [[Category: Proteinsase k]] | ||
[[Category: Synthetic peptide]] | [[Category: Synthetic peptide]] | ||
Revision as of 01:47, 26 December 2014
Crystal structure of the complex of proteinase K with a specific lactoferrin peptide Val-Leu-Leu-His at 1.93 A resolutionCrystal structure of the complex of proteinase K with a specific lactoferrin peptide Val-Leu-Leu-His at 1.93 A 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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