› 1fp1

X-ray diffraction
1.82Å resolution

CRYSTAL STRUCTURE ANALYSIS OF CHALCONE O-METHYLTRANSFERASE

Released:
DOI: 10.2210/pdb1fp1/pdb
PDB entry 1fp1 coloured by chain, front view.
PDB entry 1fp1 coloured by chain, side view.
PDB entry 1fp1 coloured by chain, top view.
Source organism: Medicago sativa
Primary publication:
Structures of two natural product methyltransferases reveal the basis for substrate specificity in plant O-methyltransferases.
Zubieta C, He XZ, Dixon RA, Noel JP
Nat Struct Biol 8 271-9 (2001)
PMID: 11224575

Function and Biology Details

Reactions catalysed: 
S-adenosyl-L-methionine + isoliquiritigenin = S-adenosyl-L-homocysteine + 2'-O-methylisoliquiritigenin
S-adenosyl-L-methionine + licodione = S-adenosyl-L-homocysteine + 2'-O-methyllicodione
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161075 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoliquiritigenin 2'-O-methyltransferase Chain: D
Molecule details ›
Chain: D
Length: 372 amino acids
Theoretical weight: 41.18 KDa
Source organism: Medicago sativa
Expression system: Escherichia coli
UniProt:
  • Canonical: P93324 (Residues: 1-372; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
1 bound ligand:
Ligand HCC 1 x HCC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 125.119Å b: 53.793Å c: 73.39Å
α: 90° β: 124.92° γ: 90°
R-values:
R R work R free
0.26 0.226 0.263
Expression system: Escherichia coli

Quick links

Citations

26 review citations

Natural products and plant disease resistance.
Dixon RA. (2001)
25 more

5 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
4 more