› 1cuh

X-ray diffraction
1.75Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132745 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cutinase 1 Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 22.25 KDa
Source organism: Fusarium vanettenii
Expression system: Escherichia coli
UniProt:
  • Canonical: P00590 (Residues: 17-230; Coverage: 100%)
Gene names: CUT1, CUTA
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: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 37Å b: 64.2Å c: 71.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.163 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Cutinase: from molecular level to bioprocess development.
Carvalho et al. (1999)
2 more

2 mentions without citation

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