Structure 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 · 2 distinct chains · 60% helix, 8% strand (DSSP).

Ligands and binding sites

• PBW · (1~{S},4~{S},5~{R})-6-(hydroxymethyl)cyclohexane-1,2,3, 4,5-pentol · ligand · 2 copies · chains A, B
• M96 · (1~{S},2~{R},3~{S},4~{R},5~{R})-5-(hydroxymethyl) cyclohexane-1,2,3,4-tetrol · ligand · 2 copies · chains A, B
• MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A, B
• 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

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

2 interfaces between chains.

• A–B · 489 Ų buried · 8 hydrogen bonds · protein-protein
• B–E · 179 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 6ZBX · Structure of the catalytic domain of the Bacillus circulans alpha-1,6 Mannanase in… · 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 6ZBX · PDBe 6ZBX · UniProt Q9Z4P9