3de6: Difference between revisions

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<StructureSection load='3de6' size='340' side='right'caption='[[3de6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3de6' size='340' side='right'caption='[[3de6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3de6]] 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=3DE6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DE6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3de6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DE6 FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d9q|3d9q]], [[3ddz|3ddz]], [[3de0|3de0]], [[3de1|3de1]], [[3de2|3de2]], [[3de3|3de3]], [[3de4|3de4]], [[3de5|3de5]], [[3de7|3de7]]</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=3de6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3de6 OCA], [https://pdbe.org/3de6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3de6 RCSB], [https://www.ebi.ac.uk/pdbsum/3de6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3de6 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3de6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3de6 OCA], [http://pdbe.org/3de6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3de6 RCSB], [http://www.ebi.ac.uk/pdbsum/3de6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3de6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] Hydrolyzes keratin at aromatic and hydrophobic residues.  
[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] 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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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/3de6_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/3de6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Proteinase|Proteinase]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Engyodontium album]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidase K]]
[[Category: Parengyodontium album]]
[[Category: Nicolini, C]]
[[Category: Nicolini C]]
[[Category: Pechkova, E]]
[[Category: Pechkova E]]
[[Category: Tripathi, S K]]
[[Category: Tripathi SK]]
[[Category: Alpha beta protein]]
[[Category: Calcium]]
[[Category: Hydrolase]]
[[Category: Metal-binding]]
[[Category: Protease]]
[[Category: Serine protease]]
[[Category: Zymogen]]

Latest revision as of 08:45, 17 October 2024

Proteinase K by Classical hanging drop method after the third step of high X-Ray dose on ESRF ID23-1 beamlineProteinase K by Classical hanging drop method after the third step of high X-Ray dose on ESRF ID23-1 beamline

Structural highlights

3de6 is a 1 chain structure with sequence from Parengyodontium album. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRTK_PARAQ 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.

Publication Abstract from PubMed

A detailed analysis of structural and intensity changes induced by X-ray radiation is presented for two types of proteinase K crystals: crystal grown by classical hanging drop method and those grown by Langmuir-Blodgett (LB) nanotemplate. The comparison of various parameters (e.g. intensity per sigma ratio, unit-cell volume, number of unique reflections, B-factors) and electron density maps as a function of radiation dose, demonstrates that crystals, grown by the LB nanotemplate method, appear to be more resistant against radiation damage than crystals grown by the classical hanging drop method.

Radiation stability of proteinase K crystals grown by LB nanotemplate method.,Pechkova E, Tripathi S, Ravelli RB, McSweeney S, Nicolini C J Struct Biol. 2009 Dec;168(3):409-18. Epub 2009 Aug 15. PMID:19686853[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Pechkova E, Tripathi S, Ravelli RB, McSweeney S, Nicolini C. Radiation stability of proteinase K crystals grown by LB nanotemplate method. J Struct Biol. 2009 Dec;168(3):409-18. Epub 2009 Aug 15. PMID:19686853 doi:10.1016/j.jsb.2009.08.005

3de6, resolution 2.20Å

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OCA