4pyi

X-ray diffraction
1.35Å resolution

human apo COMT

Released:
Source organism: Homo sapiens
Primary publication:
Mapping the conformational space accessible to catechol-O-methyltransferase.
Acta Crystallogr D Biol Crystallogr 70 2163-74 (2014)
PMID: 25084335

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-149486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catechol O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 24.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21964 (Residues: 51-271; Coverage: 82%)
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: SLS BEAMLINE X10SA
Spacegroup: P1
Unit cell:
a: 31.596Å b: 42.638Å c: 43.663Å
α: 115.03° β: 95.35° γ: 108.98°
R-values:
R R work R free
0.165 0.162 0.213
Expression system: Escherichia coli