› 3g0i

X-ray diffraction
2.1Å resolution

Complex of Aspergillus niger epoxide hydrolase with valpromide (2-propylpentanamide)

Released:
DOI: 10.2210/pdb3g0i/pdb
PDB entry 3g0i coloured by chain, front view.
PDB entry 3g0i coloured by chain, side view.
PDB entry 3g0i coloured by chain, top view.
Source organism: Aspergillus niger
Primary publication:
Directed evolution of an enantioselective epoxide hydrolase: uncovering the source of enantioselectivity at each evolutionary stage.
Reetz MT, Bocola M, Wang LW, Sanchis J, Cronin A, Arand M, Zou J, Archelas A, Bottalla AL, Naworyta A, Mowbray SL
J Am Chem Soc 131 7334-43 (2009)
PMID: 19469578

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-194080 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epoxide hydrolase N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 44.12 KDa
Source organism: Aspergillus niger
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UR30 (Residues: 5-396; Coverage: 99%)
Gene name: hyl1
Sequence domains: Epoxide hydrolase N terminus
Structure domains: alpha/beta hydrolase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 62.985Å b: 89.655Å c: 75.812Å
α: 90° β: 105.31° γ: 90°
R-values:
R R work R free
0.176 0.175 0.222
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Directed evolution drives the next generation of biocatalysts.
Turner NJ. (2009)
10 more

3 mentions without citation

How mutational epistasis impairs predictability in protein evolution and design.
Miton et al. (2016)
2 more