2duj: Difference between revisions

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<StructureSection load='2duj' size='340' side='right'caption='[[2duj]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
<StructureSection load='2duj' size='340' side='right'caption='[[2duj]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2duj]] 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=2DUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DUJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2duj]] is a 2 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=2DUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DUJ 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>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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]] 1.67&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hd4|2hd4]], [[2dqk|2dqk]]</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>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</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=2duj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2duj OCA], [https://pdbe.org/2duj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2duj RCSB], [https://www.ebi.ac.uk/pdbsum/2duj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2duj ProSAT]</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=2duj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2duj OCA], [http://pdbe.org/2duj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2duj RCSB], [http://www.ebi.ac.uk/pdbsum/2duj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2duj 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/du/2duj_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/du/2duj_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]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Engyodontium album]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidase K]]
[[Category: Parengyodontium album]]
[[Category: Gupta, D]]
[[Category: Gupta D]]
[[Category: Sharma, S]]
[[Category: Sharma S]]
[[Category: Singh, A K]]
[[Category: Singh AK]]
[[Category: Singh, N]]
[[Category: Singh N]]
[[Category: Singh, T P]]
[[Category: Singh TP]]
[[Category: Somvanshi, R K]]
[[Category: Somvanshi RK]]
[[Category: Complex]]
[[Category: Hydrolase]]
[[Category: Synthetic peptide]]

Latest revision as of 10:55, 30 October 2024

Crystal structure of the complex formed between proteinase K and a synthetic peptide Leu-Leu-Phe-Asn-Asp at 1.67 A resolutionCrystal structure of the complex formed between proteinase K and a synthetic peptide Leu-Leu-Phe-Asn-Asp at 1.67 A resolution

Structural highlights

2duj is a 2 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 1.67Å
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.

See Also

2duj, resolution 1.67Å

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