4c3t: Difference between revisions
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''' | ==The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme== | ||
<StructureSection load='4c3t' size='340' side='right' caption='[[4c3t]], [[Resolution|resolution]] 1.69Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4c3t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermovibrio_ammonificans Thermovibrio ammonificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3T FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3t RCSB], [http://www.ebi.ac.uk/pdbsum/4c3t PDBsum]</span></td></tr> | |||
<table> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Carbonate dehydratase]] | |||
[[Category: Thermovibrio ammonificans]] | |||
[[Category: Berg, S.]] | |||
[[Category: Isupov, M.]] | |||
[[Category: James, P.]] | |||
[[Category: Kotlar, H.]] | |||
[[Category: Lioliou, M.]] | |||
[[Category: Littlechild, J.]] | |||
[[Category: Sayer, C.]] | |||
[[Category: Acetazolamide]] | |||
[[Category: Carbon dioxide capture]] | |||
[[Category: Lyase]] | |||
[[Category: Thermal stability]] | |||
[[Category: Thermophilic]] | |||
Revision as of 10:05, 10 September 2014
The Carbonic anhydrase from Thermovibrio ammonificans reveals an interesting intermolecular disulfide contributing to increasing thermal stability of this enzyme
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