› 3gbs

X-ray diffraction
1.75Å resolution

Function and Biology Details

Reaction catalysed: 
Cutin + H(2)O = cutin monomers
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156687 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cutinase 1 Chain: A
Molecule details ›
Chain: A
Length: 197 amino acids
Theoretical weight: 20.64 KDa
Source organism: Aspergillus oryzae
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P52956 (Residues: 17-213; Coverage: 100%)
Gene names: AO090005000029, CutL1, cutL
Sequence domains: Cutinase
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P3221
Unit cell:
a: 45.299Å b: 45.299Å c: 157.111Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.194 0.199
Expression system: Komagataella pastoris

Quick links

Citations

7 review citations

Cutinase: characteristics, preparation, and application.
Chen et al. (2013)
6 more

13 mentions without citation

Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET.
Magalhães et al. (2021)
12 more