Structure of the D125N mutant of the catalytic domain of the bacillus circulans alpha-1,6 mannanase in complex with an alpha-1,6-alpha- manno-cyclophellitol carbasugar-stabilised trisaccharide inhibitor

Structure

x-ray diffraction · 1 distinct chain · 63% helix, 8% strand (DSSP).

Ligands and binding sites

• QE8 · (1~{R},2~{R},3~{R},4~{S},5~{R})-4-[[(1~{S},2~{S},3~{S}, 4~{R},5~{R})-5-(hydroxymethyl)-2,3,4-tris(oxidanyl) cyclohexyl]oxymethyl]cyclohexane-1,2,3,5-tetrol · ligand · chains A
• MAN · alpha-D-mannopyranose · sugar · chains A
• EDO · 1,2-ethanediol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

• 6ZBM · Structure of the D125N mutant of the catalytic domain of the Bacillus circulans alpha-1,6… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt Q9Z4P9
• Elsewhere: RCSB PDB 6ZBM · PDBe 6ZBM · UniProt Q9Z4P9