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==Crystal structure of the complex of proteinase K with auramine at 1.8A resolution==
==Crystal structure of the complex of proteinase K with auramine at 1.8A resolution==
<StructureSection load='2pyz' size='340' side='right' caption='[[2pyz]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
<StructureSection load='2pyz' size='340' side='right'caption='[[2pyz]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== 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 [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium 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 [https://proteopedia.org/fgij/fg.htm?mol=2PYZ FirstGlance]. <br>
</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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pwb|2pwb]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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=2pyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pyz OCA], [https://pdbe.org/2pyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pyz RCSB], [https://www.ebi.ac.uk/pdbsum/2pyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pyz 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=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 ==
== 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]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/2pyz_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/py/2pyz_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>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2pyz ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Proteinase|Proteinase]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Engyodontium album]]
[[Category: Large Structures]]
[[Category: Peptidase K]]
[[Category: Parengyodontium album]]
[[Category: Bhushan, A]]
[[Category: Bhushan A]]
[[Category: Kaur, P]]
[[Category: Kaur P]]
[[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: Sinha, M]]
[[Category: Sinha M]]
[[Category: Enzyme activity]]
[[Category: Hydrolase]]
[[Category: Inhibition]]

Latest revision as of 10:45, 9 October 2024

Crystal structure of the complex of proteinase K with auramine at 1.8A resolutionCrystal structure of the complex of proteinase K with auramine at 1.8A resolution

Structural highlights

2pyz 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 1.79Å
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

2pyz, resolution 1.79Å

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