X-ray diffraction
2.85Å resolution

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


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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
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
  • 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:
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 R work R free
0.219 0.215 0.295
Expression system: Escherichia coli