› 5fhq

X-ray diffraction
1.63Å resolution

Crystal structure of (WT) Rat Catechol-O-Methyltransferase in complex with AdoMet and 3,5-dinitrocatechol (DNC)

Released:
DOI: 10.2210/pdb5fhq/pdb
PDB entry 5fhq coloured by chain, front view.
PDB entry 5fhq coloured by chain, side view.
PDB entry 5fhq coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase.
Law BJ, Bennett MR, Thompson ML, Levy C, Shepherd SA, Leys D, Micklefield J
OpenAccess logo Angew Chem Int Ed Engl 55 2683-7 (2016)
PMID: 26797714

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 Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 23.98 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P22734 (Residues: 46-258; Coverage: 81%)
Gene name: Comt
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
2 bound ligands:
Ligand DNC 1 x DNC
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3221
Unit cell:
a: 50.72Å b: 50.72Å c: 167.55Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.155 0.188
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Biotechnological production of aromatic compounds of the extended shikimate pathway from renewable biomass.
Lee et al. (2017)
4 more

1 mention without citation

Effects of Active-Site Modification and Quaternary Structure on the Regioselectivity of Catechol-O-Methyltransferase.
Law et al. (2016)