5er1
From Proteopedia
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| - | [[ | + | ==A rational approach to the design of antihypertensives. X-ray studies of complexes between aspartic proteinases and aminoalcohol renin inhibitors== |
| + | <StructureSection load='5er1' size='340' side='right' caption='[[5er1]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5er1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ER1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ER1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0HT:METHYL+N-[(2S,3S)-3-AMINO-2-HYDROXY-5-METHYLHEXYL]-L-VALYL-L-ISOLEUCYL-L-PHENYLALANINATE'>0HT</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30] </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=5er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5er1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5er1 RCSB], [http://www.ebi.ac.uk/pdbsum/5er1 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/5er1_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </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]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Yeast enolase (2-phospho-D-glycerate hydrolyase, EC 4.2.1.11) has been crystallized by vapor diffusion and equilibrium dialysis of solutions of ammonium sulfate. The crystals with the dimer have 2-fold axial symmetry and appear to be suitable for high-resolution X-ray diffraction analysis. Our potential heavy-atom derivative of the native crystals has been prepared. | ||
| - | + | Crystallization and preliminary crystallographic data for a tetragonal form of yeast enolase.,Lebioda L, Brewer JM J Mol Biol. 1984 Nov 25;180(1):213-5. PMID:6392568<ref>PMID:6392568</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Pepsin|Pepsin]] | *[[Pepsin|Pepsin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Cryphonectria parasitica]] | [[Category: Cryphonectria parasitica]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
| - | [[Category: Blundell, T L | + | [[Category: Blundell, T L]] |
| - | [[Category: Cooper, J B | + | [[Category: Cooper, J B]] |
| - | [[Category: Foundling, S I | + | [[Category: Foundling, S I]] |
[[Category: Acid proteinase]] | [[Category: Acid proteinase]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
Revision as of 16:47, 10 December 2014
A rational approach to the design of antihypertensives. X-ray studies of complexes between aspartic proteinases and aminoalcohol renin inhibitors
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