2xhn

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<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=2xhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xhn RCSB], [http://www.ebi.ac.uk/pdbsum/2xhn PDBsum]</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=2xhn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xhn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xhn RCSB], [http://www.ebi.ac.uk/pdbsum/2xhn PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/RHGB_ASPAC RHGB_ASPAC]] Pectinolytic enzyme that has a positive effect in the apple hot-mash liquefaction process. This endolyase hydrolyzes the alpha-L-rhamnopyranosyl-(1,4)-alpha-D-galacturonopyranosyl glycosidic linkage by beta-elimination, thereby generating oligosaccharides terminating at the non-reducing end with a hex-4-enopyranosyluronic acid residue.<ref>PMID:8587995</ref> <ref>PMID:9576783</ref> <ref>PMID:20851126</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 14:42, 25 December 2014

RHAMNOGALACTURONAN LYASE FROM ASPERGILLUS ACULEATUS K150A ACTIVE SITE MUTANT

2xhn, resolution 1.52Å

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