4c28: Difference between revisions

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 ==Crystal structure of Trypanosoma cruzi CYP51 bound to the inhibitor (R)-N-(3-(1H-indol-3-yl)-1-oxo-1-(pyridin-4-ylamino)propan-2-yl)-4-(4-(4-chlorophenyl)piperazin-1-yl)-2-fluorobenzamide.==
-<StructureSection load='4c28' size='340' side='right' caption='[[4c28]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
+<StructureSection load='4c28' size='340' side='right'caption='[[4c28]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4c28]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C28 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4c28]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C28 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TW5:(R)-N-(3-(1H-INDOL-3-YL)-1-OXO-1-(PYRIDIN-4-YLAMINO)PROPAN-2-YL)-4-(4-(4-CHLOROPHENYL)PIPERAZIN-1-YL)-2-FLUOROBENZAMIDE'>TW5</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]] 2.03&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c27|4c27]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TW5:(R)-N-(3-(1H-INDOL-3-YL)-1-OXO-1-(PYRIDIN-4-YLAMINO)PROPAN-2-YL)-4-(4-(4-CHLOROPHENYL)PIPERAZIN-1-YL)-2-FLUOROBENZAMIDE'>TW5</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sterol_14-demethylase Sterol 14-demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.70 1.14.13.70] </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=4c28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c28 OCA], [https://pdbe.org/4c28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c28 RCSB], [https://www.ebi.ac.uk/pdbsum/4c28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c28 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=4c28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c28 OCA], [http://pdbe.org/4c28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c28 RCSB], [http://www.ebi.ac.uk/pdbsum/4c28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c28 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CP51_TRYCC CP51_TRYCC]] Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol (By similarity). Favors C4 dimethylated substrates, the substrate preference order is 24-methylenedihydrolanosterol > 24,25-dihydrolanosterol > lanosterol > obtusifoliol > norlanosterol.<ref>PMID:16321980</ref> [UniProtKB:P0A512]
+[https://www.uniprot.org/uniprot/CP51_TRYCC CP51_TRYCC] Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol (By similarity). Favors C4 dimethylated substrates, the substrate preference order is 24-methylenedihydrolanosterol > 24,25-dihydrolanosterol > lanosterol > obtusifoliol > norlanosterol.<ref>PMID:16321980</ref> [UniProtKB:P0A512]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 </div>
 <div class="pdbe-citations 4c28" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Sterol 14-demethylase]]
+[[Category: Large Structures]]
-[[Category: Calvet, C M]]
+[[Category: Trypanosoma cruzi]]
-[[Category: Cameron, M D]]
+[[Category: Calvet CM]]
-[[Category: Choi, J Y]]
+[[Category: Cameron MD]]
-[[Category: Gut, J]]
+[[Category: Choi JY]]
-[[Category: Kellar, D]]
+[[Category: Gut J]]
-[[Category: McKerrow, J H]]
+[[Category: Kellar D]]
-[[Category: Podust, L M]]
+[[Category: McKerrow JH]]
-[[Category: Roush, W R]]
+[[Category: Podust LM]]
-[[Category: Siqueira-Neto, J L]]
+[[Category: Roush WR]]
-[[Category: Vieira, D F]]
+[[Category: Siqueira-Neto JL]]
-[[Category: Chagas disease]]
+[[Category: Vieira DF]]
-[[Category: Oxidoreductase]]
-[[Category: Sterol biosynthesis]]