› 2vaq

X-ray diffraction
3.01Å resolution

STRUCTURE OF STRICTOSIDINE SYNTHASE IN COMPLEX WITH INHIBITOR

Released:
DOI: 10.2210/pdb2vaq/pdb
PDB entry 2vaq coloured by chain, front view.
PDB entry 2vaq coloured by chain, side view.
PDB entry 2vaq coloured by chain, top view.
Source organism: Rauvolfia serpentina
Primary publication:
Strictosidine synthase: mechanism of a Pictet-Spengler catalyzing enzyme.
Maresh JJ, Giddings LA, Friedrich A, Loris EA, Panjikar S, Trout BL, Stöckigt J, Peters B, O'Connor SE
J Am Chem Soc 130 710-23 (2008)
PMID: 18081287

Function and Biology Details

Reaction catalysed: 
3-alpha-(S)-strictosidine + H(2)O = tryptamine + secologanin
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159354 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Strictosidine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 35.77 KDa
Source organism: Rauvolfia serpentina
Expression system: Escherichia coli
UniProt:
  • Canonical: P68175 (Residues: 23-344; Coverage: 100%)
Gene name: STR1
Sequence domains: Strictosidine synthase
Structure domains: TolB, C-terminal domain

Ligands and Environments

1 bound ligand:
Ligand VAW 2 x VAW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: R3
Unit cell:
a: 149.993Å b: 149.993Å c: 121.688Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.186 0.247
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Natural products: a continuing source of novel drug leads.
Cragg et al. (2013)
15 more

2 mentions without citation

Strictosidine synthase: mechanism of a Pictet-Spengler catalyzing enzyme.
Maresh et al. (2008)
1 more