5ngw

Glycoside hydrolase-like protein

spinqualitylabelsall models 5ngw, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ngw is a 1 chain structure with sequence from Ochrovirga pacifica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: BR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2R2JFJ2_9FLAO Publication Abstract from PubMed Algal polysaccharides of diverse structures are one of the most abundant carbon resources for heterotrophic, marine bacteria with coevolved digestive enzymes. A putative sulfo-mannan polysaccharide utilization locus, which is conserved in marine flavobacteria, contains an unusual GH99-like protein that lacks the conserved catalytic residues of glycoside hydrolase family 99. Using X-ray crystallography, we structurally characterized this protein from the marine flavobacterium Ochrovirga pacifica to help elucidate its molecular function. The structure reveals the absence of potential catalytic residues for polysaccharide hydrolysis, which-together with additional structural features-suggests this protein may be noncatalytic and involved in carbohydrate binding. Crystal structure of a marine glycoside hydrolase family 99-related protein lacking catalytic machinery.,Robb CS, Mystkowska AA, Hehemann JH Protein Sci. 2017 Dec;26(12):2445-2450. doi: 10.1002/pro.3291. Epub 2017 Nov 21. PMID:28884852 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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