7cef

X-ray diffraction
1.6Å resolution

Crystal structure of PET-degrading cutinase Cut190 /S226P/R228S/ mutant with the C-terminal three residues deletion

Released:

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: 262 amino acids
Theoretical weight: 28.85 KDa
Source organism: Saccharomonospora viridis
Expression system: Escherichia coli
UniProt:
  • Canonical: W0TJ64 (Residues: 45-304; Coverage: 86%)
Gene names: Cut190, MINT15_00360
Sequence domains: Platelet-activating factor acetylhydrolase, isoform II

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-1A
Spacegroup: P21
Unit cell:
a: 60.512Å b: 49.1Å c: 82.948Å
α: 90° β: 107.453° γ: 90°
R-values:
R R work R free
0.179 0.177 0.22
Expression system: Escherichia coli