Humanized rat catechol O-methyltransferase in complex with N-[2-[5- (1H-benzimidazol-5-yl)-4H-1,2,4-triazol-3-YL]ETHYL]-5-(4- fluorophenyl)-2,3-dihydroxybenzamide at 1.31A

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 20% strand (DSSP).

Ligands and binding sites

• 75Z · N-[2-[5-(1H-benzimidazol-5-yl)-4H-1,2,4-triazol-3-yl]ethyl]-5-(4-fluorophenyl)-2,3-dihydroxybenzamide · ligand · chains A
• D1D · (4S,5S)-1,2-dithiane-4,5-diol · ligand · chains A
• MG · Magnesium ion · metal · chains A
• CL · Chloride ion · ion · 2 copies · chains A
• SO4 · Sulfate ion · ion · chains A
• NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 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.

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

• 5P8X · humanized rat catechol O-methyltransferase in complex with… · 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 5P8X · PDBe 5P8X · UniProt P22734