› 6ix2

X-ray diffraction
1.48Å resolution

Structure of the A214C/A250I mutant of an epoxide hydrolase from Aspergillus usamii E001 (AuEH2) at 1.48 Angstroms resolution

Released:
DOI: 10.2210/pdb6ix2/pdb
PDB entry 6ix2 coloured by chain, front view.
PDB entry 6ix2 coloured by chain, side view.
PDB entry 6ix2 coloured by chain, top view.
Source organism: Aspergillus usamii
Primary publication:
Structure-Guided Regulation in the Enantioselectivity of an Epoxide Hydrolase to Produce Enantiomeric Monosubstituted Epoxides and Vicinal Diols via Kinetic Resolution.
Hu D, Hu BC, Hou XD, Zhang D, Lei YQ, Rao YJ, Wu MC
Org Lett 24 1757-1761 (2022)
PMID: 35229602

Function and Biology Details

Reaction catalysed: 
1-(4-methoxyphenyl)-N-methyl-N-((3-methyloxetan-3-yl)methyl)methanamine + H(2)O = 2-((((4-methoxyphenyl)methyl)(methyl)amino)methyl)-2-methylpropane-1,3-diol
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-197493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epoxide hydrolase N-terminal domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 431 amino acids
Theoretical weight: 48.57 KDa
Source organism: Aspergillus usamii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: T2B4K5 (Residues: 1-395; Coverage: 100%)
Gene name: EH2
Sequence domains: Epoxide hydrolase N terminus

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P21
Unit cell:
a: 57.365Å b: 51.922Å c: 133.488Å
α: 90° β: 90.97° γ: 90°
R-values:
R R work R free
0.16 0.159 0.178
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Epoxide Hydrolases: Multipotential Biocatalysts.
Bučko et al. (2023)

2 mentions without citation

Crystal structures of β-1,4-N-acetylglucosaminyltransferase 2: structural basis for inherited muscular dystrophies.
Yang et al. (2021)
1 more