4pyk

X-ray diffraction
2.22Å resolution

human COMT, double domain swap

Released:
Source organism: Homo sapiens
Primary publication:
Mapping the conformational space accessible to catechol-O-methyltransferase.
OpenAccess logo 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

Assemblies composition:
monomeric (preferred)
homo dimer
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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 54.786Å b: 66.825Å c: 128.032Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.172 0.244
Expression system: Escherichia coli