› 7cts

X-ray diffraction
1.1Å resolution

Open form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation

Released:
DOI: 10.2210/pdb7cts/pdb
PDB entry 7cts coloured by chain, front view.
PDB entry 7cts coloured by chain, side view.
PDB entry 7cts coloured by chain, top view.
Source organism: Saccharomonospora viridis
Primary publication:
Structural basis of mutants of PET-degrading enzyme from Saccharomonospora viridis AHK190 with high activity and thermal stability.
Emori M, Numoto N, Senga A, Bekker GJ, Kamiya N, Kobayashi Y, Ito N, Kawai F, Oda M
Proteins 89 502-511 (2021)
PMID: 33340163

Function and Biology Details

Reaction catalysed: 
Cutin + H(2)O = cutin monomers
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cutinase Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.89 KDa
Source organism: Saccharomonospora viridis
Expression system: Escherichia coli
UniProt:
  • Canonical: W0TJ64 (Residues: 47-304; Coverage: 85%)
Gene names: Cut190, MINT15_00360
Sequence domains: Platelet-activating factor acetylhydrolase, isoform II

Ligands and Environments

3 bound ligands:
Ligand DIO 1 x DIO
Ligand BCN 1 x BCN
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 62.623Å b: 64.984Å c: 78.453Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.143 0.142 0.162
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase.
Pfaff et al. (2022)
1 more

5 mentions without citation

Mechanism-Based Design of Efficient PET Hydrolases.
Wei et al. (2022)
4 more