This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5er1
From Proteopedia
(Difference between revisions)
| (3 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:5er1.png|left|200px]] | ||
| - | + | ==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/Crypa Crypa]. 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://proteopedia.org/fgij/fg.htm?mol=5ER1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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://proteopedia.org/fgij/fg.htm?mol=5er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5er1 OCA], [http://pdbe.org/5er1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5er1 RCSB], [http://www.ebi.ac.uk/pdbsum/5er1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5er1 ProSAT]</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/main_output.php?pdb_ID=5er1 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> | |
| - | + | <div class="pdbe-citations 5er1" style="background-color:#fffaf0;"></div> | |
| - | + | ||
==See Also== | ==See Also== | ||
*[[Pepsin|Pepsin]] | *[[Pepsin|Pepsin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Crypa]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
| - | [[Category: Blundell, T L | + | [[Category: Large Structures]] |
| - | [[Category: Cooper, J B | + | [[Category: Blundell, T L]] |
| - | [[Category: Foundling, S I | + | [[Category: Cooper, J B]] |
| + | [[Category: Foundling, S I]] | ||
[[Category: Acid proteinase]] | [[Category: Acid proteinase]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
Current revision
A rational approach to the design of antihypertensives. X-ray studies of complexes between aspartic proteinases and aminoalcohol renin inhibitors
| |||||||||||

