› 4o5t

X-ray diffraction
2.9Å resolution

Crystal structure of Diels-Alderase CE20 in complex with a product analog

Released:
DOI: 10.2210/pdb4o5t/pdb
PDB entry 4o5t coloured by chain, front view.
PDB entry 4o5t coloured by chain, side view.
PDB entry 4o5t coloured by chain, top view.
Source organism: Loligo vulgaris
Primary publication:
Impact of scaffold rigidity on the design and evolution of an artificial Diels-Alderase.
Preiswerk N, Beck T, Schulz JD, Milovník P, Mayer C, Siegel JB, Baker D, Hilvert D
Proc Natl Acad Sci U S A 111 8013-8 (2014)
PMID: 24847076

Function and Biology Details

Reaction catalysed: 
Diisopropyl fluorophosphate + H(2)O = diisopropyl phosphate + fluoride
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181980 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diisopropyl-fluorophosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.3 KDa
Source organism: Loligo vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7SIG4 (Residues: 1-35, 36-36, 37-44, 45-314; Coverage: 100%)
Sequence domains: SMP-30/Gluconolactonase/LRE-like region
Structure domains: TolB, C-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 88.65Å b: 128.94Å c: 106.53Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.228 0.288
Expression system: Escherichia coli

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Citations

18 review citations

Directed Evolution of Protein Catalysts.
Zeymer et al. (2018)
17 more

3 mentions without citation

Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.
Currin et al. (2015)
2 more