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X-ray diffraction
1.3Å resolution

Function and Biology Details

Reaction catalysed: 
(Ethylene terephthalate)(n) + H(2)O = (ethylene terephthalate)(n-1) + ethylene terephthalate
Biochemical function:
Biological process:
Cellular component:
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 Chain: A
Molecule details ›
Chain: A
Length: 272 amino acids
Theoretical weight: 28.91 KDa
Source organism: Ideonella sakaiensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0K8P6T7 (Residues: 29-290; Coverage: 100%)
Gene name: ISF6_4831
Sequence domains: Dienelactone hydrolase family

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P3121
Unit cell:
a: 86.013Å b: 86.013Å c: 88.924Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.112 0.111 0.133
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Current advances in the structural biology and molecular engineering of PETase.
Liu et al. (2023)
1 more