4oap

An Axe2 mutant (W190I), an acetyl-xylooligosaccharide esterase from Geobacillus Stearmophilus

spinqualitylabelsall models 4oap, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4oap is a 2 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.93Å Ligands: ACT, CL, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AXE2_GEOSE Acetylxylan esterase involved in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Cleaves acetyl side groups from the xylose backbone units of the hemicellulolytic polymer xylan and xylo-oligosaccharides. Hydrolyzes about 20%-30% of the available acetyl groups on fully acetylated birch wood xylan. Completely deacetylates xylobiose peracetate (fully acetylated), and is active on both the alpha- and beta-forms of the sugar. Also hydrolyzes fully acetylated methyl-beta-D-xylopyranoside and methyl-beta-D-glucopyranoside, and the synthetic substrates 2-naphthyl acetate, 4-nitrophenyl acetate, 4-methylumbelliferyl acetate, and phenyl acetate. See Also Acetylxylan esterase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA