› 7sh6

X-ray diffraction
1.44Å resolution

Crystal structure of a PET hydrolase mutant from Ideonella Sakaiensis

Released:
DOI: 10.2210/pdb7sh6/pdb
PDB entry 7sh6 coloured by chain, front view.
PDB entry 7sh6 coloured by chain, side view.
PDB entry 7sh6 coloured by chain, top view.
Source organism: Ideonella sakaiensis
Primary publication:
Machine learning-aided engineering of hydrolases for PET depolymerization.
Lu H, Diaz DJ, Czarnecki NJ, Zhu C, Kim W, Shroff R, Acosta DJ, Alexander BR, Cole HO, Zhang Y, Lynd NA, Ellington AD, Alper HS
Nature 604 662-667 (2022)
PMID: 35478237

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 Chain: A
Molecule details ›
Chain: A
Length: 292 amino acids
Theoretical weight: 30.81 KDa
Source organism: Ideonella sakaiensis
Expression system: Pseudomonas putida KT2440
UniProt:
  • Canonical: A0A0K8P6T7 (Residues: 27-290; Coverage: 100%)
Gene name: ISF6_4831
Sequence domains: Dienelactone hydrolase family

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 50.942Å b: 51.182Å c: 84.047Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.158 0.168
Expression system: Pseudomonas putida KT2440

Quick links

Citations

23 review citations

Fungal Enzymes Involved in Plastics Biodegradation.
Temporiti et al. (2022)
22 more

1 mention without citation

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