› 4nzz

X-ray diffraction
1.75Å resolution

Crystal structure of epoxide hydrolase from bacillus megaterium

Released:
DOI: 10.2210/pdb4nzz/pdb
PDB entry 4nzz coloured by chain, front view.
PDB entry 4nzz coloured by chain, side view.
PDB entry 4nzz 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: 320 amino acids
Theoretical weight: 37.09 KDa
Source organism: Priestia megaterium
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: G9BEX6 (Residues: 1-287; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 64.231Å b: 76.006Å c: 120.808Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.233
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

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

4 mentions without citation

Exploring the origins of selectivity in soluble epoxide hydrolase from Bacillus megaterium.
Serrano-Hervás et al. (2017)
3 more