› 5k0l

X-ray diffraction
2.02Å resolution

Crystal Structure of COMT in complex with 5-[5-[1-(4-methoxyphenyl)cyclopropyl]-1H-pyrazol-3-yl]-2,4-dimethyl-1,3-thiazole

Released:
DOI: 10.2210/pdb5k0l/pdb
PDB entry 5k0l coloured by chain, front view.
PDB entry 5k0l coloured by chain, side view.
PDB entry 5k0l 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-540293 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catechol O-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 219 amino acids
Theoretical weight: 24.48 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22734 (Residues: 45-263; Coverage: 83%)
Gene name: Comt
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

4 bound ligands:
Ligand MG 4 x MG
Ligand 6P2 4 x 6P2
Ligand NHE 6 x NHE
Ligand K 4 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 77.167Å b: 69.963Å c: 104.053Å
α: 90° β: 94.18° γ: 90°
R-values:
R R work R free
0.2 0.198 0.249
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Methyltransferases: Functions and Applications.
Abdelraheem et al. (2022)
3 more

1 mention without citation

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