3caq: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:3caq.jpg|left|200px]]


<!--
==Crystal structure of 5beta-reductase (AKR1D1) in complex with NADPH==
The line below this paragraph, containing "STRUCTURE_3caq", creates the "Structure Box" on the page.
<StructureSection load='3caq' size='340' side='right'caption='[[3caq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3caq]] is a 2 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=3CAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CAQ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
{{STRUCTURE_3caq| PDB=3caq |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3caq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3caq OCA], [https://pdbe.org/3caq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3caq RCSB], [https://www.ebi.ac.uk/pdbsum/3caq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3caq ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/AK1D1_HUMAN AK1D1_HUMAN] Defects in AKR1D1 are the cause of congenital bile acid synthesis defect type 2 (CBAS2) [MIM:[https://omim.org/entry/235555 235555]; also known as cholestasis with delta(4)-3-oxosteroid 5-beta-reductase deficiency. Patients with this liver disease show absence or low levels of chenodeoxycholic acid and cholic acid in plasma and urine.<ref>PMID:12970144</ref> <ref>PMID:15030995</ref>
== Function ==
[https://www.uniprot.org/uniprot/AK1D1_HUMAN AK1D1_HUMAN] Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates.
== 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/ca/3caq_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=3caq ConSurf].
<div style="clear:both"></div>


===Crystal structure of 5beta-reductase (AKR1D1) in complex with NADPH===
==See Also==
 
*[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]]
 
== References ==
==About this Structure==
<references/>
3CAQ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAQ OCA].
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Breton, R]]
[[Category: Large Structures]]
[[Category: Cantin, L]]
[[Category: Breton R]]
[[Category: Faucher, F]]
[[Category: Cantin L]]
[[Category: 5b-dhp]]
[[Category: Faucher F]]
[[Category: 5b-red]]
[[Category: 5b-reductase]]
[[Category: 5beta-reductase]]
[[Category: Akr]]
[[Category: Akr1d1]]
[[Category: Aldo-keto reductase]]
[[Category: Androstenedione]]
[[Category: Bile acid catabolism]]
[[Category: Cytoplasm]]
[[Category: Disease mutation]]
[[Category: Lipid metabolism]]
[[Category: Nadp]]
[[Category: Nadph]]
[[Category: Oxidoreductase]]
[[Category: Steroid metabolism]]
[[Category: Substrate inhibition]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 10 15:02:57 2008''