Crystal structure of the bacterial cellulose secretion regulator bcse, residues 217-523, with bound C-di-gmp.

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 21% strand (DSSP).

Ligands and binding sites

• C2E · 9,9'-[(2r,3r,3as,5s,7ar,9r,10r,10as,12s,14ar)-3,5,10, 12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3, 2-D:3',2'-J][1,3,7,9,2, 8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) · ligand · chains A, B
• GOL · Glycerol · additive · 2 copies · chains A, B

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.

Interfaces

1 interface between chains.

• A–B · 185 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 19 modified (engineered).

Compared structures

• 6TJ0 · Crystal structure of the bacterial cellulose secretion regulator BcsE, residues 217-523… · the same entry in another collection · chain A against A, TM-score 1.00
• P37657 · AlphaFold monomer V2.0 prediction for cyclic di-gmp binding protein bcse (P37657) · a predicted model of the same protein · chain B against A, TM-score 0.58

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 P37657
• Elsewhere: RCSB PDB 6TJ0 · PDBe 6TJ0 · UniProt P37657