› 5icf

X-ray diffraction
1.8Å resolution

Crystal structure of (S)-norcoclaurine 6-O-methyltransferase with S-adenosyl-L-homocysteine and sanguinarine

Released:
DOI: 10.2210/pdb5icf/pdb
PDB entry 5icf coloured by chain, front view.
PDB entry 5icf coloured by chain, side view.
PDB entry 5icf coloured by chain, top view.
Source organism: Thalictrum flavum subsp. glaucum
Primary publication:
Crystal structure of norcoclaurine-6-O-methyltransferase, a key rate-limiting step in the synthesis of benzylisoquinoline alkaloids.
Robin AY, Giustini C, Graindorge M, Matringe M, Dumas R
Plant J 87 641-53 (2016)
PMID: 27232113

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + (RS)-norcoclaurine = S-adenosyl-L-homocysteine + (RS)-coclaurine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176904 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
(RS)-norcoclaurine 6-O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 352 amino acids
Theoretical weight: 39.53 KDa
Source organism: Thalictrum flavum subsp. glaucum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5C9L7 (Residues: 3-350; Coverage: 99%)
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
5 bound ligands:
Ligand SAU 1 x SAU
Ligand K 2 x K
Ligand NA 1 x NA
Ligand EDO 13 x EDO
Ligand DMS 2 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21212
Unit cell:
a: 73.34Å b: 109.09Å c: 40.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.156 0.192
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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