6qn0: Difference between revisions

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'''Unreleased structure'''


The entry 6qn0 is ON HOLD
==Three dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamide==
 
<StructureSection load='6qn0' size='340' side='right'caption='[[6qn0]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
Authors: Dvinskis, E., Leitans, J., Tars, K.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6qn0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QN0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QN0 FirstGlance]. <br>
Description: Three dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamide
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=J8Q:~{N}-butyl-4-chloranyl-2-(2-phenylethylsulfanyl)-5-sulfamoyl-benzamide'>J8Q</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] </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=6qn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qn0 OCA], [http://pdbe.org/6qn0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qn0 RCSB], [http://www.ebi.ac.uk/pdbsum/6qn0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qn0 ProSAT]</span></td></tr>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/CAH12_HUMAN CAH12_HUMAN]] Defects in CA12 are the cause of hyperchlorhidrosis isolated (HCHLH) [MIM:[http://omim.org/entry/143860 143860]]. HCHLH is a disorder characterized by excessive sweating and increased sweat chloride levels. Affected individuals suffer from episodes of hyponatremic dehydration and report increased amounts of visible salt precipitates in sweat.<ref>PMID:21035102</ref> 
== Function ==
[[http://www.uniprot.org/uniprot/CAH12_HUMAN CAH12_HUMAN]] Reversible hydration of carbon dioxide.
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Carbonate dehydratase]]
[[Category: Large Structures]]
[[Category: Dvinskis, E]]
[[Category: Dvinskis, E]]
[[Category: Leitans, J]]
[[Category: Leitans, J]]
[[Category: Tars, K]]
[[Category: Tars, K]]
[[Category: Lyase]]

Revision as of 12:20, 26 February 2020

Three dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamideThree dimensional structure of human carbonic anhydrase XII in complex with benzenesulfonamide

Structural highlights

6qn0 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Carbonate dehydratase, with EC number 4.2.1.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[CAH12_HUMAN] Defects in CA12 are the cause of hyperchlorhidrosis isolated (HCHLH) [MIM:143860]. HCHLH is a disorder characterized by excessive sweating and increased sweat chloride levels. Affected individuals suffer from episodes of hyponatremic dehydration and report increased amounts of visible salt precipitates in sweat.[1]

Function

[CAH12_HUMAN] Reversible hydration of carbon dioxide.

References

  1. Feldshtein M, Elkrinawi S, Yerushalmi B, Marcus B, Vullo D, Romi H, Ofir R, Landau D, Sivan S, Supuran CT, Birk OS. Hyperchlorhidrosis caused by homozygous mutation in CA12, encoding carbonic anhydrase XII. Am J Hum Genet. 2010 Nov 12;87(5):713-20. doi: 10.1016/j.ajhg.2010.10.008. Epub, 2010 Oct 28. PMID:21035102 doi:10.1016/j.ajhg.2010.10.008

6qn0, resolution 1.89Å

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