Crystal structure of the catalytic domain of the inosine monophosphate dehydrogenase from bacillus anthracis in the complex with a product imp and the inhibitor P182

Structure

x-ray diffraction · 3 distinct chains · 37% helix, 22% strand (DSSP).

Ligands and binding sites

• IMP · Inosinic acid · ligand · 4 copies · chains A, B, C, D
• 8L1 · N-{4-chloro-3-[4-(trifluoromethyl)-1,3-thiazol-2-yl]phenyl}-N'-(2-{3-[(1E)-N-hydroxyethanimidoyl]phenyl}propan-2-yl)urea · ligand · 4 copies · chains A, D, B, C
• K · Potassium ion · metal · 4 copies · chains A, D, C, B
• GOL · Glycerol · additive · 2 copies · chains B, C

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

Pockets

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

Interfaces

4 interfaces between chains.

• B–C · 2590 Ų buried · 38 hydrogen bonds · protein-protein
• A–D · 2553 Ų buried · 39 hydrogen bonds · protein-protein
• B–D · 2552 Ų buried · 40 hydrogen bonds · protein-protein
• A–C · 2542 Ų buried · 37 hydrogen bonds · protein-protein

Compared structures

• 5UUV · Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from… · 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 Q81W29
• Elsewhere: RCSB PDB 5UUV · PDBe 5UUV · UniProt Q81W29