1h37: Difference between revisions

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 <StructureSection load='1h37' size='340' side='right'caption='[[1h37]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h37]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_27009 Atcc 27009]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H37 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h37]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H37 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H37 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=R02:{4-[((1S,2S)-2-{[ALLYL(CYCLOPROPYL)AMINO]METHYL}CYCLOPROPYL)METHOXY]PHENYL}(4-BROMOPHENYL)METHANONE'>R02</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]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gsz|1gsz]], [[1h35|1h35]], [[1h36|1h36]], [[1h39|1h39]], [[1h3a|1h3a]], [[1h3b|1h3b]], [[1h3c|1h3c]], [[1sqc|1sqc]], [[2sqc|2sqc]], [[3sqc|3sqc]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=R02:{4-[((1S,2S)-2-{[ALLYL(CYCLOPROPYL)AMINO]METHYL}CYCLOPROPYL)METHOXY]PHENYL}(4-BROMOPHENYL)METHANONE'>R02</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Squalene--hopene_cyclase Squalene--hopene cyclase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.17 5.4.99.17] </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=1h37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h37 OCA], [https://pdbe.org/1h37 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h37 RCSB], [https://www.ebi.ac.uk/pdbsum/1h37 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h37 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SQHC_ALIAD SQHC_ALIAD] Catalyzes the cyclization of squalene into hopene.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1h37 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The binding structures of 11 human oxidosqualene cyclase inhibitors designed as cholesterol-lowering agents were determined for the squalene-hopene cyclase from Alicyclobacillus acidocaldarius, which is the only structurally known homologue of the human enzyme. The complexes were produced by cocrystallization, and the structures were elucidated by X-ray diffraction analyses. All inhibitors were bound in the large active center cavity. The detailed binding structures are presented and discussed in the light of the IC50 values of these 11 as well as 17 other inhibitors. They provide a consistent picture for the inhibition of the bacterial enzyme and can be used to adjust and improve homology models of the human enzyme. The detailed active center structures of the two enzymes are too different to show an IC50 correlation.
-Binding structures and potencies of oxidosqualene cyclase inhibitors with the homologous squalene-hopene cyclase.,Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE J Med Chem. 2003 May 22;46(11):2083-92. PMID:12747780<ref>PMID:12747780</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1h37" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Squalene-hopene cyclase|Squalene-hopene cyclase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 27009]]
+[[Category: Alicyclobacillus acidocaldarius]]
 [[Category: Large Structures]]
-[[Category: Squalene--hopene cyclase]]
+[[Category: Aebi JD]]
-[[Category: Aebi, J D]]
+[[Category: Dehmlow H]]
-[[Category: Dehmlow, H]]
+[[Category: Lenhart A]]
-[[Category: Lenhart, A]]
+[[Category: Morand OH]]
-[[Category: Morand, O H]]
+[[Category: Reinert DJ]]
-[[Category: Reinert, D J]]
+[[Category: Schulz GE]]
-[[Category: Schulz, G E]]
+[[Category: Weihofen WA]]
-[[Category: Weihofen, W A]]
-[[Category: Cholesterol biosynthesis]]
-[[Category: Inhibitor]]
-[[Category: Isomerase]]
-[[Category: Monotopic membrane protein]]