X-ray diffraction
1.58Å resolution

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


Function and Biology Details

Reaction catalysed:
(Ethylene terephthalate)(n) + H(2)O = (ethylene terephthalate)(n-1) + ethylene terephthalate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
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
  • 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 R work R free
0.17 0.169 0.184
Expression system: Escherichia coli