3dax: Difference between revisions

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<StructureSection load='3dax' size='340' side='right'caption='[[3dax]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3dax' size='340' side='right'caption='[[3dax]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3dax]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DAX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3DAX FirstGlance]. <br>
<table><tr><td colspan='2'>[[3dax]] 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=3DAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DAX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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]] 2.15&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP7A1, CYP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cholesterol_7-alpha-monooxygenase Cholesterol 7-alpha-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.17 1.14.13.17] </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=3dax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dax OCA], [https://pdbe.org/3dax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dax RCSB], [https://www.ebi.ac.uk/pdbsum/3dax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dax ProSAT]</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=3dax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dax OCA], [http://pdbe.org/3dax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dax RCSB], [http://www.ebi.ac.uk/pdbsum/3dax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dax ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CP7A1_HUMAN CP7A1_HUMAN]] Catalyzes a rate-limiting step in cholesterol catabolism and bile acid biosynthesis by introducing a hydrophilic moiety at position 7 of cholesterol. Important for cholesterol homeostasis.<ref>PMID:19965590</ref>
[https://www.uniprot.org/uniprot/CP7A1_HUMAN CP7A1_HUMAN] Catalyzes a rate-limiting step in cholesterol catabolism and bile acid biosynthesis by introducing a hydrophilic moiety at position 7 of cholesterol. Important for cholesterol homeostasis.<ref>PMID:19965590</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cholesterol 7-alpha-monooxygenase]]
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith CH]]
[[Category: Bochkarev, A]]
[[Category: Bochkarev A]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Dombrovski, L]]
[[Category: Dombrovski L]]
[[Category: Dong, A]]
[[Category: Dong A]]
[[Category: Edwards, A M]]
[[Category: Edwards AM]]
[[Category: Loppnau, P]]
[[Category: Loppnau P]]
[[Category: Park, H]]
[[Category: Park H]]
[[Category: Structural genomic]]
[[Category: Strushkevich NV]]
[[Category: Strushkevich, N V]]
[[Category: Tempel W]]
[[Category: Tempel, W]]
[[Category: Wilkstrom M]]
[[Category: Wilkstrom, M]]
[[Category: Cholesterol]]
[[Category: Cholesterol 7-alpha hydroxylase]]
[[Category: Cholesterol metabolism]]
[[Category: Cytochrome p450]]
[[Category: Endoplasmic reticulum]]
[[Category: Heme]]
[[Category: Iron]]
[[Category: Lipid metabolism]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Microsome]]
[[Category: Monooxygenase]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: Polymorphism]]
[[Category: Sgc]]
[[Category: Steroid metabolism]]

Latest revision as of 15:43, 30 August 2023

Crystal structure of human CYP7A1Crystal structure of human CYP7A1

Structural highlights

3dax is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CP7A1_HUMAN Catalyzes a rate-limiting step in cholesterol catabolism and bile acid biosynthesis by introducing a hydrophilic moiety at position 7 of cholesterol. Important for cholesterol homeostasis.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. Li T, Chanda D, Zhang Y, Choi HS, Chiang JY. Glucose stimulates cholesterol 7alpha-hydroxylase gene transcription in human hepatocytes. J Lipid Res. 2010 Apr;51(4):832-42. doi: 10.1194/jlr.M002782. Epub 2009 Oct 28. PMID:19965590 doi:http://dx.doi.org/10.1194/jlr.M002782

3dax, resolution 2.15Å

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OCA