5yfe

X-ray diffraction
1.39Å resolution

Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase PETase from I. sakaiensis

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 28.69 KDa
Source organism: Ideonella sakaiensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0K8P6T7 (Residues: 27-290; Coverage: 100%)
Gene name: ISF6_4831
Sequence domains: Dienelactone hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P212121
Unit cell:
a: 50.945Å b: 56.644Å c: 80.611Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.235
Expression system: Escherichia coli BL21(DE3)