The glucuronoyl esterase OTCE15A S267A variant from opitutus terrae in complex with benzyl D-glucuronoate and D-glucuronate

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 20% strand (DSSP).

Ligands and binding sites

• TMO · trimethylamine oxide · ligand · 7 copies · chains A, B
• M55 · benzyl alpha-D-glucopyranuronate · ligand · chains A
• GCU · alpha-D-glucopyranuronic acid · sugar · 2 copies · chains A, B
• MG · Magnesium ion · metal · chains A
• CL · Chloride ion · ion · chains A, B
• EDO · 1,2-ethanediol · additive · 34 copies · chains A, B
• PEG · Di(hydroxyethyl)ether · additive · 6 copies · chains A, B
• PGE · Triethylene glycol · additive · 5 copies · chains A, B
• DMS · Dimethyl sulfoxide · additive · 5 copies · chains A, B
• PG4 · Tetraethylene glycol · additive · chains A, B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 801 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

• 6T0E · The glucuronoyl esterase OtCE15A S267A variant from Opitutus terrae in complex with… · 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 B1ZMF4
• Elsewhere: RCSB PDB 6T0E · PDBe 6T0E · UniProt B1ZMF4