Rat catechol O-methyltransferase in complex with a catechol-type, N6-methyladenine-containing bisubstrate inhibitor

Structure

x-ray diffraction · resolution 1.3 · 1 distinct chain · 46% helix, 22% strand (DSSP).

Ligands and binding sites

• 542 · N-[(E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-(6-methylaminopurin-9-yl)oxolan-2-yl]prop-2-enyl]-5-(4-fluorophenyl)-2,3-dihydroxy-benzamide · ligand · chains A
• MG · Magnesium ion · metal · chains A
• CL · Chloride ion · ion · 3 copies · chains A
• SO4 · Sulfate ion · ion · 2 copies · chains A
• CXS · 3-cyclohexyl-1-propylsulfonic acid · additive · 2 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Compared structures

• 3HVH · Rat catechol O-methyltransferase in complex with a catechol-type, N6… · the same entry in another collection · chain A against A, TM-score 1.00
• P22734 · AlphaFold monomer V2.0 prediction for catechol O-methyltransferase (P22734) · a predicted model of the same protein · 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 P22734
• Elsewhere: RCSB PDB 3HVH · PDBe 3HVH · UniProt P22734