› 4pyj

X-ray diffraction
1.9Å resolution

human apo-COMT, single domain swap

Released:
DOI: 10.2210/pdb4pyj/pdb
PDB entry 4pyj coloured by chain, front view.
PDB entry 4pyj coloured by chain, side view.
PDB entry 4pyj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mapping the conformational space accessible to catechol-O-methyltransferase.
Ehler A, Benz J, Schlatter D, Rudolph MG
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
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-539996 (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

3 bound ligands:
Ligand NA 1 x NA
Ligand MG 1 x MG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 54.882Å b: 67.165Å c: 128.827Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.198 0.263
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Molecular recognition in chemical and biological systems.
Persch et al. (2015)
1 more

1 mention without citation

Mapping the conformational space accessible to catechol-O-methyltransferase.
Ehler et al. (2014)