4fdh: Difference between revisions
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New page: '''Unreleased structure''' The entry 4fdh is ON HOLD Authors: Strushkevich, N., Shen, L., Tempel, W., Arrowsmith, C., Edwards, A., Usanov, S.A., Park, H.-W. Description: Structure of h... |
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The entry | ==Structure of human aldosterone synthase, CYP11B2, in complex with fadrozole== | ||
<StructureSection load='4fdh' size='340' side='right'caption='[[4fdh]], [[Resolution|resolution]] 2.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fdh]] is a 12 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=4FDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FDH 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]] 2.71Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0T3:4-[(5R)-5,6,7,8-TETRAHYDROIMIDAZO[1,5-A]PYRIDIN-5-YL]BENZONITRILE'>0T3</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=4fdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdh OCA], [https://pdbe.org/4fdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fdh RCSB], [https://www.ebi.ac.uk/pdbsum/4fdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fdh ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/C11B2_HUMAN C11B2_HUMAN] Familial hyperreninemic hypoaldosteronism type 1;Familial hyperaldosteronism type I. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The molecular defect causing hyperaldosteronism familial 1 is an anti-Lepore-type fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the promoting part of CYP11B1, ACTH-sensitive, and the coding part of CYP11B2. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C11B2_HUMAN C11B2_HUMAN] Preferentially catalyzes the conversion of 11-deoxycorticosterone to aldosterone via corticosterone and 18-hydroxycorticosterone.<ref>PMID:23322723</ref> | |||
==See Also== | |||
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith C]] | |||
[[Category: Edwards A]] | |||
[[Category: Park H-W]] | |||
[[Category: Shen L]] | |||
[[Category: Strushkevich N]] | |||
[[Category: Tempel W]] | |||
[[Category: Usanov SA]] | |||
Latest revision as of 14:15, 1 March 2024
Structure of human aldosterone synthase, CYP11B2, in complex with fadrozoleStructure of human aldosterone synthase, CYP11B2, in complex with fadrozole
Structural highlights
DiseaseC11B2_HUMAN Familial hyperreninemic hypoaldosteronism type 1;Familial hyperaldosteronism type I. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The molecular defect causing hyperaldosteronism familial 1 is an anti-Lepore-type fusion of the CYP11B1 and CYP11B2 genes. The hybrid gene has the promoting part of CYP11B1, ACTH-sensitive, and the coding part of CYP11B2. FunctionC11B2_HUMAN Preferentially catalyzes the conversion of 11-deoxycorticosterone to aldosterone via corticosterone and 18-hydroxycorticosterone.[1] See AlsoReferences
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