› 5kok

X-ray diffraction
1.79Å resolution

Pavine N-methyltransferase in complex with Tetrahydropapaverine and S-adenosylhomocysteine pH 7.25

Released:
DOI: 10.2210/pdb5kok/pdb
PDB entry 5kok coloured by chain, front view.
PDB entry 5kok coloured by chain, side view.
PDB entry 5kok coloured by chain, top view.
Source organism: Thalictrum flavum subsp. glaucum
Primary publication:
Structural and Functional Studies of Pavine N-Methyltransferase from Thalictrum flavum Reveal Novel Insights into Substrate Recognition and Catalytic Mechanism.
Torres MA, Hoffarth E, Eugenio L, Savtchouk J, Chen X, Morris JS, Facchini PJ, Ng KK
J Biol Chem 291 23403-23415 (2016)
PMID: 27573242

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + (+-)-pavine = S-adenosyl-L-homocysteine + N-methylpavine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pavine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 397 amino acids
Theoretical weight: 46.44 KDa
Source organism: Thalictrum flavum subsp. glaucum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: C3SBW0 (Residues: 1-356; Coverage: 100%)
Gene name: PavNMT
Sequence domains: Mycolic acid cyclopropane synthetase

Ligands and Environments

3 bound ligands:
Ligand SAH 2 x SAH
Ligand S9T 2 x S9T
Ligand R9T 2 x R9T
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 53.776Å b: 71.637Å c: 95.226Å
α: 90° β: 99.21° γ: 90°
R-values:
R R work R free
0.165 0.163 0.199
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Recent advances in methyltransferase biocatalysis.
Bennett et al. (2017)
2 more

8 mentions without citation

Molecular Origins of Functional Diversity in Benzylisoquinoline Alkaloid Methyltransferases.
Morris et al. (2019)
7 more