› 8b26

X-ray diffraction
2.42Å resolution

Dihydroprecondylocarpine acetate synthase 2 from Tabernanthe iboga

Released:
DOI: 10.2210/pdb8b26/pdb
PDB entry 8b26 coloured by chain, front view.
PDB entry 8b26 coloured by chain, side view.
PDB entry 8b26 coloured by chain, top view.
Source organism: Tabernanthe iboga
Primary publication:
Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.
Langley C, Tatsis E, Hong B, Nakamura Y, Paetz C, Stevenson CE, Basquin J, Lawson DM, Caputi L, O'Connor SE
OpenAccess logo Angew Chem Int Ed Engl (2022)
PMID: 36198083

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-105325 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Enoyl reductase (ER) domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 365 amino acids
Theoretical weight: 39.28 KDa
Source organism: Tabernanthe iboga
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A5B8X8Z0 (Residues: 1-365; Coverage: 100%)
Sequence domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 74.422Å b: 78.124Å c: 131.207Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Recycling Upstream Redox Enzymes Expands the Regioselectivity of Cycloaddition in Pseudo-Aspidosperma Alkaloid Biosynthesis.
Kamileen et al. (2022)
2 more

1 mention without citation

Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.
Langley et al. (2022)