1est: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
==THE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE STRUCTURE OF ALPHA-CHYMOTRYPSIN==
==THE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE STRUCTURE OF ALPHA-CHYMOTRYPSIN==
<StructureSection load='1est' size='340' side='right' caption='[[1est]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1est' size='340' side='right'caption='[[1est]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1est]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EST FirstGlance]. <br>
<table><tr><td colspan='2'>[[1est]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EST FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TSU:PARA-TOLUENE+SULFONATE'>TSU</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]] 2.5&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TSU:PARA-TOLUENE+SULFONATE'>TSU</scene></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=1est FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1est OCA], [http://pdbe.org/1est PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1est RCSB], [http://www.ebi.ac.uk/pdbsum/1est PDBsum]</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=1est FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1est OCA], [https://pdbe.org/1est PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1est RCSB], [https://www.ebi.ac.uk/pdbsum/1est PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1est ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG]] Acts upon elastin.  
[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin.
== 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/es/1est_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/es/1est_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1est ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Elastase|Elastase]]
*[[Elastase 3D structures|Elastase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pancreatic elastase]]
[[Category: Large Structures]]
[[Category: Pig]]
[[Category: Sus scrofa]]
[[Category: Sawyer, L]]
[[Category: Sawyer L]]
[[Category: Shotton, D M]]
[[Category: Shotton DM]]
[[Category: Watson, H C]]
[[Category: Watson HC]]
[[Category: Hydrolase]]

Latest revision as of 13:06, 20 March 2024

THE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE STRUCTURE OF ALPHA-CHYMOTRYPSINTHE ATOMIC STRUCTURE OF CRYSTALLINE PORCINE PANCREATIC ELASTASE AT 2.5 ANGSTROMS RESOLUTION. COMPARISONS WITH THE STRUCTURE OF ALPHA-CHYMOTRYPSIN

Structural highlights

1est is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CELA1_PIG Acts upon elastin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1est, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA