3czv

<StructureSection load='3czv' size='340' side='right' caption='[[3czv]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[3czv]] 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=3CZV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CZV FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AZM:5-ACETAMIDO-1,3,4-THIADIAZOLE-2-SULFONAMIDE'>AZM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ca2|1ca2]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CA13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<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=3czv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3czv OCA], [http://pdbe.org/3czv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3czv RCSB], [http://www.ebi.ac.uk/pdbsum/3czv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3czv ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/CAH13_HUMAN CAH13_HUMAN]] Reversible hydration of carbon dioxide.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The cytosolic isoform XIII is a recently discovered member of the human carbonic anhydrase (hCA, EC 4.2.1.1) family. It is selectively expressed among other tissues in the reproductive organs, where it may control pH and ion balance regulation, ensuring thus proper fertilization conditions. The authors report here the X-ray crystallographic structure of this isozyme in the unbound state and in complex with a classical sulfonamide inhibitor, namely acetazolamide. A detailed comparison of the obtained structural data with those already reported for other CA isozymes provides novel insights into the catalytic properties of the members of this protein family. On the basis of the inhibitory properties of acetazolamide against various cytosolic/transmembrane isoforms and the structural differences detected within the active site of the various CA isoforms, further prospects for the design of isozyme-specific CA inhibitors are here proposed. Proteins 2008. (c) 2008 Wiley-Liss, Inc.

Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide.,Di Fiore A, Monti SM, Hilvo M, Parkkila S, Romano V, Scaloni A, Pedone C, Scozzafava A, Supuran CT, De Simone G Proteins. 2008 Jul 10. PMID:18618712<ref>PMID:18618712</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3czv" style="background-color:#fffaf0;"></div>

*[[Carbonic anhydrase|Carbonic anhydrase]]

[[Category: Carbonate dehydratase]]

[[Category: Human]]

[[Category: Fiore, A Di]]

[[Category: Simone, G De]]

[[Category: Carbonic anhydrase]]

[[Category: Protein-inhibitor complex]]