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

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 23% strand (DSSP).

Ligands and binding sites

• 705 · N-[(E)-3-[(2R,3S,4R,5R)-3,4-dihydroxy-5-(6-propylaminopurin-9-yl)oxolan-2-yl]prop-2-enyl]-5-(4-fluorophenyl)-2,3-dihydroxy-benzamide · ligand · 2 copies · chains A, B
• MG · Magnesium ion · metal · 2 copies · chains A, B
• CL · Chloride ion · ion · chains A
• BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 402 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

• 3HVJ · Rat catechol O-methyltransferase in complex with a catechol-type… · 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 3HVJ · PDBe 3HVJ · UniProt P22734