2zlb

X-ray diffraction
2.2Å resolution

Crystal structure of APO form of rat catechol-O-methyltransferase

Released:
Source organism: Rattus norvegicus
Entry author: Tsuji E

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catechol O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 223 amino acids
Theoretical weight: 24.92 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P22734 (Residues: 44-264; Coverage: 84%)
  • Best match: P22734-2 (Residues: 1-221)
Gene name: Comt
Sequence domains: O-methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32B2
Spacegroup: P3121
Unit cell:
a: 56.262Å b: 56.262Å c: 117.483Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.179 0.237
Expression system: Escherichia coli