› 6eqh

X-ray diffraction
1.58Å resolution

Crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis in spacegroup C2221

Released:
DOI: 10.2210/pdb6eqh/pdb
PDB entry 6eqh coloured by chain, front view.
PDB entry 6eqh coloured by chain, side view.
PDB entry 6eqh coloured by chain, top view.
Source organism: Ideonella sakaiensis
Primary publication:
Characterization and engineering of a plastic-degrading aromatic polyesterase.
Austin HP, Allen MD, Donohoe BS, Rorrer NA, Kearns FL, Silveira RL, Pollard BC, Dominick G, Duman R, El Omari K, Mykhaylyk V, Wagner A, Michener WE, Amore A, Skaf MS, Crowley MF, Thorne AW, Johnson CW, Woodcock HL, McGeehan JE, Beckham GT
Proc Natl Acad Sci U S A 115 E4350-E4357 (2018)
PMID: 29666242

Function and Biology Details

Reaction catalysed: 
(Ethylene terephthalate)(n) + H(2)O = (ethylene terephthalate)(n-1) + ethylene terephthalate
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-102331 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly(ethylene terephthalate) hydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 298 amino acids
Theoretical weight: 31.34 KDa
Source organism: Ideonella sakaiensis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0K8P6T7 (Residues: 1-290; Coverage: 100%)
Gene name: ISF6_4831
Sequence domains: Dienelactone hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2221
Unit cell:
a: 52.702Å b: 234.134Å c: 165.123Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.169 0.184
Expression system: Escherichia coli

Quick links

Citations

59 review citations

Beyond Mechanical Recycling: Giving New Life to Plastic Waste.
Vollmer et al. (2020)
58 more

6 mentions without citation

Current knowledge on enzymatic PET degradation and its possible application to waste stream management and other fields.
Kawai et al. (2019)
5 more