› 6gky

X-ray diffraction
2.85Å resolution

Crystal structure of Coclaurine N-Methyltransferase (CNMT) bound to N-methylheliamine and SAH

Released:
DOI: 10.2210/pdb6gky/pdb
PDB entry 6gky coloured by chain, front view.
PDB entry 6gky coloured by chain, side view.
PDB entry 6gky coloured by chain, top view.
Source organism: Coptis japonica
Primary publication:
Structure and Biocatalytic Scope of Coclaurine N-Methyltransferase.
Bennett MR, Thompson ML, Shepherd SA, Dunstan MS, Herbert AJ, Smith DRM, Cronin VA, Menon BRK, Levy C, Micklefield J
Angew Chem Int Ed Engl 57 10600-10604 (2018)
PMID: 29791083

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline = S-adenosyl-L-homocysteine + N-methyl-(RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188201 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coclaurine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 41.07 KDa
Source organism: Coptis japonica
Expression system: Escherichia coli
UniProt:
  • Canonical: Q948P7 (Residues: 7-357; Coverage: 98%)
Gene name: cnmt
Sequence domains: Mycolic acid cyclopropane synthetase

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:
Ligand F2Z 2 x F2Z
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 48.295Å b: 95.957Å c: 154.567Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.215 0.295
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Enzyme-mediated bioorthogonal technologies: catalysts, chemoselective reactions and recent methyltransferase applications.
Jalali et al. (2021)
4 more

2 mentions without citation

Structure and Biocatalytic Scope of Coclaurine N-Methyltransferase.
Bennett et al. (2018)
1 more