› 5k0b

X-ray diffraction
2.36Å resolution

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

Released:
DOI: 10.2210/pdb5k0b/pdb
PDB entry 5k0b coloured by chain, front view.
PDB entry 5k0b coloured by chain, side view.
PDB entry 5k0b 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 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 218 amino acids
Theoretical weight: 24.32 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22734 (Residues: 45-261; Coverage: 82%)
Gene name: Comt
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

6 bound ligands:
Ligand 6PS 8 x 6PS
Ligand PO4 17 x PO4
Ligand K 8 x K
Ligand CL 5 x CL
Ligand CXS 7 x CXS
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P61
Unit cell:
a: 222.095Å b: 222.095Å c: 123.085Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.157 0.155 0.195
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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