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2x8f

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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=2x8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x8f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x8f RCSB], [http://www.ebi.ac.uk/pdbsum/2x8f 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=2x8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x8f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x8f RCSB], [http://www.ebi.ac.uk/pdbsum/2x8f PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/B3FRL6_BACSU B3FRL6_BACSU]] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of the alpha-1,5-L-arabinan to produce arabino-oligosaccharides and L-arabinose. It is also active toward linear branched sugar beet arabinan, and pectin from apple.<ref>PMID:18408032</ref> <ref>PMID:20883454</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 07:53, 25 December 2014

NATIVE STRUCTURE OF ENDO-1,5-ALPHA-L-ARABINANASES FROM BACILLUS SUBTILIS

2x8f, resolution 1.90Å

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