› 4io0

X-ray diffraction
2.9Å resolution

Crystal structure of F128A mutant of an epoxide hydrolase from Bacillus megaterium complexed with its product (R)-3-[1]naphthyloxy-propane-1,2-diol

Released:
DOI: 10.2210/pdb4io0/pdb
PDB entry 4io0 coloured by chain, front view.
PDB entry 4io0 coloured by chain, side view.
PDB entry 4io0 coloured by chain, top view.
Source organism: Priestia megaterium
Primary publication:
Engineering of an epoxide hydrolase for efficient bioresolution of bulky pharmaco substrates.
Kong XD, Yuan S, Li L, Chen S, Xu JH, Zhou J
Proc Natl Acad Sci U S A 111 15717-22 (2014)
PMID: 25331869

Function and Biology Details

Reaction catalysed: 
A pyrimidine 5'-nucleotide + H(2)O = D-ribose 5-phosphate + a pyrimidine base
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124658 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 304 amino acids
Theoretical weight: 35.21 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli
UniProt:
  • Canonical: G9BEX6 (Residues: 1-287; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand RN1 2 x RN1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P41212
Unit cell:
a: 109.64Å b: 109.64Å c: 117.496Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.156 0.232
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Role of conformational dynamics in the evolution of novel enzyme function.
Maria-Solano et al. (2018)
5 more

3 mentions without citation

Engineering of an epoxide hydrolase for efficient bioresolution of bulky pharmaco substrates.
Kong et al. (2014)
2 more