Crystal structure at 1.8 ångströms of seleno methionyled crh, the bacillus subtilis catabolite repression containing protein crh reveals an unexpected swapping domain as an untertwinned dimer

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 30% strand (DSSP).

Ligands and binding sites

• SO4 · Sulfate ion · ion · 10 copies · chains A, D, B, C
• GOL · Glycerol · additive · 9 copies · chains A, B, D, C

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

5 interfaces between chains.

• C–D · 2257 Ų buried · 57 hydrogen bonds · protein-protein
• A–B · 2232 Ų buried · 58 hydrogen bonds · protein-protein
• A–D · 426 Ų buried · 6 hydrogen bonds · protein-protein
• B–C · 413 Ų buried · 5 hydrogen bonds · protein-protein
• A–C · 116 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

• 1MO1 · Crystal structure at 1.8 ångströms of seleno methionyled crh, the bacillus subtilis… · the same entry in another collection · chain D against D, TM-score 1.00
• O06976 · AlphaFold monomer V2.0 prediction for hpr-like protein crh (O06976) · a predicted model of the same protein · chain D against A, TM-score 0.76

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 O06976
• Elsewhere: RCSB PDB 1MO1 · PDBe 1MO1 · UniProt O06976