› 2efj

X-ray diffraction
2Å resolution

The structure of 1,7 dimethylxanthine methyltransferase

Released:
DOI: 10.2210/pdb2efj/pdb
PDB entry 2efj coloured by chain, front view.
PDB entry 2efj coloured by chain, side view.
PDB entry 2efj coloured by chain, top view.
Source organism: Coffea canephora
Primary publication:
The structure of two N-methyltransferases from the caffeine biosynthetic pathway.
McCarthy AA, McCarthy JG
Plant Physiol 144 879-89 (2007)
PMID: 17434991

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + 1,7-dimethylxanthine = S-adenosyl-L-homocysteine + 1,3,7-trimethylxanthine
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-107292 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3,7-dimethylxanthine N-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 384 amino acids
Theoretical weight: 43.41 KDa
Source organism: Coffea canephora
Expression system: Escherichia coli
UniProt:
  • Canonical: A4GE70 (Residues: 1-384; Coverage: 100%)
Gene names: DXMT, GSCOC_T00011062001
Sequence domains: SAM dependent carboxyl methyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
1 bound ligand:
Ligand 37T 1 x 37T
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2221
Unit cell:
a: 50.16Å b: 105.63Å c: 140.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.22 0.276
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Alkaloid biosynthesis: metabolism and trafficking.
Ziegler et al. (2008)
9 more

6 mentions without citation

Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases.
Lashley et al. (2022)
5 more