5ll5: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
m Protected "5ll5" [edit=sysop:move=sysop]
No edit summary
 
(3 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 5ll5 is ON HOLD
==Crystal structure of human carbonic anhydrase isozyme XII with 4-(1H-benzimidazol-1-ylacetyl)benzenesulfonamide==
<StructureSection load='5ll5' size='340' side='right'caption='[[5ll5]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ll5]] 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=5LL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LL5 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]] 1.42&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6YH:4-[2-(benzimidazol-1-yl)ethanoyl]benzenesulfonamide'>6YH</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5ll5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ll5 OCA], [https://pdbe.org/5ll5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ll5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ll5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ll5 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/CAH12_HUMAN CAH12_HUMAN] Defects in CA12 are the cause of hyperchlorhidrosis isolated (HCHLH) [MIM:[https://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 ==
[https://www.uniprot.org/uniprot/CAH12_HUMAN CAH12_HUMAN] Reversible hydration of carbon dioxide.


Authors: Smirnov, A., Manakova, E., Grazulis, S.
==See Also==
 
*[[Carbonic anhydrase 3D structures|Carbonic anhydrase 3D structures]]
Description: Crystal structure of human carbonic anhydrase isozyme XII with 4-(1H-benzimidazol-1-ylacetyl)benzenesulfonamide
== References ==
[[Category: Unreleased Structures]]
<references/>
[[Category: Grazulis, S]]
__TOC__
[[Category: Smirnov, A]]
</StructureSection>
[[Category: Manakova, E]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Grazulis S]]
[[Category: Manakova E]]
[[Category: Smirnov A]]

Latest revision as of 21:32, 18 October 2023

Crystal structure of human carbonic anhydrase isozyme XII with 4-(1H-benzimidazol-1-ylacetyl)benzenesulfonamideCrystal structure of human carbonic anhydrase isozyme XII with 4-(1H-benzimidazol-1-ylacetyl)benzenesulfonamide

Structural highlights

5ll5 is a 4 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 1.42Å
Ligands:, ,
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.

See Also

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

5ll5, resolution 1.42Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA