› 5k03

X-ray diffraction
1.81Å resolution

Crystal Structure of COMT in complex with 2,6-dimethyl-3-(1H-pyrazol-3-yl)imidazo[1,2-a]pyridine

Released:
DOI: 10.2210/pdb5k03/pdb
PDB entry 5k03 coloured by chain, front view.
PDB entry 5k03 coloured by chain, side view.
PDB entry 5k03 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Design of Potent and Druglike Nonphenolic Inhibitors for Catechol O-Methyltransferase Derived from a Fragment Screening Approach Targeting the S-Adenosyl-l-methionine Pocket.
Lerner C, Jakob-Roetne R, Buettelmann B, Ehler A, Rudolph M, Rodríguez Sarmiento RM
J Med Chem 59 10163-10175 (2016)
PMID: 27685665

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a catechol = S-adenosyl-L-homocysteine + a guaiacol
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catechol O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 23.99 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22734 (Residues: 46-259; Coverage: 81%)
Gene name: Comt
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

2 bound ligands:
Ligand 6P4 1 x 6P4
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 33.357Å b: 59.67Å c: 106.395Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Recent Developments in New Therapeutic Agents against Alzheimer and Parkinson Diseases: In-Silico Approaches.
Cruz-Vicente et al. (2021)
3 more

1 mention without citation

Cosolvent Simulations with Fragment-Bound Proteins Identify Hot Spots to Direct Lead Growth.
Lal Gupta et al. (2022)