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3na0
From Proteopedia
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| - | [[Image:3na0.png|left|200px]] | ||
| - | + | ==Crystal structure of human CYP11A1 in complex with 20,22-dihydroxycholesterol== | |
| - | + | <StructureSection load='3na0' size='340' side='right'caption='[[3na0]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3na0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NA0 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2DC:(3ALPHA,8ALPHA,22R)-CHOLEST-5-ENE-3,20,22-TRIOL'>2DC</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=3na0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3na0 OCA], [https://pdbe.org/3na0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3na0 RCSB], [https://www.ebi.ac.uk/pdbsum/3na0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3na0 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Disease == | |
| - | + | [https://www.uniprot.org/uniprot/CP11A_HUMAN CP11A_HUMAN] Inherited isolated adrenal insufficiency due to CYP11A1 deficiency;46,XY disorder of sex development - adrenal insufficiency due to CYP11A1 deficiency. The disease is caused by mutations affecting the gene represented in this entry. | |
| - | + | == Function == | |
| - | < | + | [https://www.uniprot.org/uniprot/CP11A_HUMAN CP11A_HUMAN] Catalyzes the side-chain cleavage reaction of cholesterol to pregnenolone.<ref>PMID:21636783</ref> |
| - | + | == 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/na/3na0_consurf.spt"</scriptWhenChecked> | |
| - | == | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| - | [[3na0]] is a 4 chain structure | + | <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=3na0 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Ferredoxin]] | + | *[[Ferredoxin 3D structures|Ferredoxin 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Arrowsmith | + | [[Category: Large Structures]] |
| - | [[Category: Botchkarev | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Bountra | + | [[Category: Botchkarev A]] |
| - | [[Category: Edwards | + | [[Category: Bountra C]] |
| - | [[Category: MacKenzie | + | [[Category: Edwards AM]] |
| - | [[Category: Park | + | [[Category: MacKenzie F]] |
| - | + | [[Category: Park H]] | |
| - | [[Category: Strushkevich | + | [[Category: Strushkevich NV]] |
| - | [[Category: Tempel | + | [[Category: Tempel W]] |
| - | [[Category: Weigelt | + | [[Category: Weigelt JU]] |
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Current revision
Crystal structure of human CYP11A1 in complex with 20,22-dihydroxycholesterol
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