› 6i3c

X-ray diffraction
1.34Å resolution

Crystal structure of Human soluble catechol O-methyltransferase in complex with 3,5-dinitrocatechol and S-adensoyl-L-methionine

Released:
DOI: 10.2210/pdb6i3c/pdb
PDB entry 6i3c coloured by chain, front view.
PDB entry 6i3c coloured by chain, side view.
PDB entry 6i3c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-O-methyltransferase.
Czarnota S, Johannissen LO, Baxter NJ, Rummel F, Wilson AL, Cliff MJ, Levy CW, Scrutton NS, Waltho JP, Hay S
ACS Catal 9 4394-4401 (2019)
PMID: 31080692

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-149486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Catechol O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 25.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21964 (Residues: 52-271; Coverage: 81%)
Gene name: COMT
Sequence domains: O-methyltransferase

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 43.694Å b: 61.749Å c: 46.071Å
α: 90° β: 116.42° γ: 90°
R-values:
R R work R free
0.136 0.134 0.17
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Functional roles of enzyme dynamics in accelerating active site chemistry: Emerging techniques and changing concepts.
Gao et al. (2022)
2 more

2 mentions without citation

Equatorial Active Site Compaction and Electrostatic Reorganization in Catechol-O-methyltransferase.
Czarnota et al. (2019)
1 more