Crystal structure of inosine 5'-monophosphate dehydrogenase from clostridium perfringens complexed with imp and P200

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
• 8L4 · 3-(2-{[(4-chlorophenyl)carbamoyl]amino}propan-2-yl)-N-hydroxybenzene-1-carboximidamide · ligand · 4 copies · chains A, C, B, D
• K · Potassium ion · metal · 2 copies · chains B, D, C
• MG · Magnesium ion · metal · chains B
• PEG · Di(hydroxyethyl)ether · additive · 6 copies · chains A, B, C, D
• PGE · Triethylene glycol · additive · 5 copies · chains A, C, B, D
• EDO · 1,2-ethanediol · additive · 2 copies · chains A, B, C, D
• PG4 · Tetraethylene glycol · additive · chains B, D

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

Pockets

18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Interfaces

4 interfaces between chains.

• A–B · 2570 Ų buried · 42 hydrogen bonds · protein-protein
• A–C · 2507 Ų buried · 40 hydrogen bonds · protein-protein
• C–D · 2500 Ų buried · 37 hydrogen bonds · protein-protein
• B–D · 2478 Ų buried · 40 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (acetylation).

Compared structures

• 5UZS · Crystal Structure of Inosine 5'-monophosphate Dehydrogenase from Clostridium perfringens… · 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 A0A0H2YRZ7
• Elsewhere: RCSB PDB 5UZS · PDBe 5UZS · UniProt A0A0H2YRZ7