› 4evi

X-ray diffraction
2.02Å resolution

Crystal Structure Analysis of Coniferyl Alcohol 9-O-Methyltransferase from Linum Nodiflorum in Complex with Coniferyl Alcohol 9-Methyl Ether and S -Adenosyl-L-Homocysteine

Released:
DOI: 10.2210/pdb4evi/pdb
PDB entry 4evi coloured by chain, front view.
PDB entry 4evi coloured by chain, side view.
PDB entry 4evi coloured by chain, top view.
Source organism: Linum nodiflorum
Primary publication:
Structural analysis of coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum reveals a novel active-site environment.
Wolters S, Neeb M, Berim A, Schulze Wischeler J, Petersen M, Heine A
Acta Crystallogr D Biol Crystallogr 69 888-900 (2013)
PMID: 23633600

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-501079 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coniferyl alcohol 9-O-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 388 amino acids
Theoretical weight: 43.43 KDa
Source organism: Linum nodiflorum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A6XNE6 (Residues: 1-368; Coverage: 100%)
Gene name: CA9OMT
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SAH 1 x SAH
Ligand C9M 1 x C9M
Ligand GOL 4 x GOL
Ligand N7I 1 x N7I
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P212121
Unit cell:
a: 75.842Å b: 105.042Å c: 108.983Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.176 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

One-Pot Biocatalytic In Vivo Methylation-Hydroamination of Bioderived Lignin Monomers to Generate a Key Precursor to L-DOPA.
Galman et al. (2022)
2 more

1 mention without citation

Structural analysis of coniferyl alcohol 9-O-methyltransferase from Linum nodiflorum reveals a novel active-site environment.
Wolters et al. (2013)