› 8ibm

X-ray diffraction
2.2Å resolution

Sulfate bound 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/pdb8ibm/pdb
PDB entry 8ibm coloured by chain, front view.
PDB entry 8ibm coloured by chain, side view.
PDB entry 8ibm coloured by chain, top view.
Source organism: Saccharomonospora viridis
Primary publication:
Improvement of thermostability and activity of PET-degrading enzyme Cut190 towards a detailed understanding and application of the enzymatic reaction mechanism.
Numoto N, Kamiya N, Oda M
Biorxiv (2023)

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 Chains: A, B
Molecule details ›
Chains: A, B
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

2 bound ligands:
Ligand CA 2 x CA
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P3
Unit cell:
a: 83.755Å b: 83.755Å c: 64.752Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.234 0.267
Expression system: Escherichia coli

Quick links