Crystal structure of comt in complex with 3-cyclopropyl-5-methyl-4- phenyl-1,2,4-triazole

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 21% strand (DSSP).

Ligands and binding sites

• 72N · 3-cyclopropyl-5-methyl-4-phenyl-1,2,4-triazole · ligand · 5 copies · chains A, B, C, D
• NA · Sodium ion · metal · 3 copies · chains A, B, C
• K · Potassium ion · metal · chains D
• CL · Chloride ion · ion · chains B

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

Pockets

15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–D · 786 Ų buried · 9 hydrogen bonds · protein-protein
• B–C · 751 Ų buried · 10 hydrogen bonds · protein-protein
• A–B · 417 Ų buried · 2 hydrogen bonds · protein-protein
• C–D · 408 Ų buried · 5 hydrogen bonds · protein-protein
• B–D · 256 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

• 5LQJ · Crystal Structure of COMT in complex with 3-cyclopropyl-5-methyl-4-phenyl-1,2,4-triazole · the same entry in another collection · chain D against D, TM-score 1.00
• P22734 · AlphaFold monomer V2.0 prediction for catechol O-methyltransferase (P22734) · a predicted model of the same protein · chain C against A, TM-score 0.98

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 5LQJ · PDBe 5LQJ · UniProt P22734