5koc

X-ray diffraction
2.29Å resolution

Pavine N-methyltransferase in complex with S-adenosylmethionine pH 7

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (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%)
Sequence domains: Mycolic acid cyclopropane synthetase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 54.572Å b: 72.005Å c: 96.247Å
α: 90° β: 98.97° γ: 90°
R-values:
R R work R free
0.189 0.186 0.248
Expression system: Escherichia coli BL21(DE3)