› 2cut

X-ray diffraction
1.9Å resolution

CUTINASE, A LIPOLYTIC ENZYME WITH A PREFORMED OXYANION HOLE

Released:
DOI: 10.2210/pdb2cut/pdb
PDB entry 2cut coloured by chain, front view.
PDB entry 2cut coloured by chain, side view.
PDB entry 2cut coloured by chain, top view.
Source organism: Fusarium vanettenii
Primary publication:
Cutinase, a lipolytic enzyme with a preformed oxyanion hole.
Martinez C, Nicolas A, van Tilbeurgh H, Egloff MP, Cudrey C, Verger R, Cambillau C
Biochemistry 33 83-9 (1994)
PMID: 8286366

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: 198 amino acids
Theoretical weight: 20.58 KDa
Source organism: Fusarium vanettenii
Expression system: Not provided
UniProt:
  • Canonical: P00590 (Residues: 31-228; Coverage: 93%)
Gene names: CUT1, CUTA
Sequence domains: Cutinase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand DEP 1 x DEP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 40.3Å b: 61.1Å c: 72.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Not provided

Quick links

Citations

14 review citations

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

4 mentions without citation

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