1pek

<StructureSection load='1pek' size='340' side='right' caption='[[1pek]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[1pek]] is a 3 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=1PEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PEK FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1pek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pek OCA], [http://pdbe.org/1pek PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pek RCSB], [http://www.ebi.ac.uk/pdbsum/1pek PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] Hydrolyzes keratin at aromatic and hydrophobic residues.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1pek_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The crystal structure of a transition state/product complex formed by the interaction between proteinase K and the substrate analogue N-Ac-L-Pro-L-Ala-L-Pro-L-Phe-D-Ala-L-Ala-NH2 has been determined at a resolution of 2.2 A and refined to an R-factor of 0.165 for 12,725 reflections. The inhibitor forms a stable complex through a series of hydrogen bonds with protein atoms and water molecules. The inhibitor is hydrolyzed between Phe 4I and D-Ala5I (I indicates inhibitor). The two fragments are separated by a distance of 3.07 A between the carbonyl carbon and the main chain nitrogen. Both fragments remain bound to the protein. The N-terminal fragment occupies subsites S5 to S1, whereas the C-terminal part is bound in S1' and S2', the first time that electron density for a substrate analogue has been observed in the P1' and P2' sites of a subtilisin-like enzyme. The flexible segments of the substrate recognition sites Gly100-Tyr104 and Ser132-Gly136 move appreciably to accommodate the inhibitor. Biochemical results indicate an inhibition by this specifically designed peptide of 95%.

Structure of the complex of proteinase K with a substrate analogue hexapeptide inhibitor at 2.2-A resolution.,Betzel C, Singh TP, Visanji M, Peters K, Fittkau S, Saenger W, Wilson KS J Biol Chem. 1993 Jul 25;268(21):15854-8. PMID:8340410<ref>PMID:8340410</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1pek" style="background-color:#fffaf0;"></div>

*[[Proteinase|Proteinase]]

[[Category: Engyodontium album]]

[[Category: Peptidase K]]

[[Category: Betzel, C]]

[[Category: Fittkau, S]]

[[Category: Peters, K]]

[[Category: Saenger, W]]

[[Category: Singh, T P]]

[[Category: Visanji, M]]

[[Category: Wilson, K S]]

[[Category: Hydrolase-hydrolase inhibitor complex]]