› 1oxm

X-ray diffraction
2.3Å resolution

STRUCTURE OF CUTINASE

Released:
DOI: 10.2210/pdb1oxm/pdb
PDB entry 1oxm coloured by chain, front view.
PDB entry 1oxm coloured by chain, side view.
PDB entry 1oxm coloured by chain, top view.
Source organism: Fusarium vanettenii
Primary publication:
Crystal structure of cutinase covalently inhibited by a triglyceride analogue.
Longhi S, Mannesse M, Verheij HM, De Haas GH, Egmond M, Knoops-Mouthuy E, Cambillau C
Protein Sci 6 275-86 (1997)
PMID: 9041628

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 214 amino acids
Theoretical weight: 22.28 KDa
Source organism: Fusarium vanettenii
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00590 (Residues: 17-230; Coverage: 100%)
Gene names: CUT1, CUTA
Sequence domains: Cutinase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand TC4 2 x TC4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 37.2Å b: 69.2Å c: 73.3Å
α: 90° β: 93.8° γ: 90°
R-values:
R R work R free
0.163 0.163 0.227
Expression system: Saccharomyces cerevisiae

Quick links

Citations

5 review citations

Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases.
Jaeger et al. (1999)
4 more

3 mentions without citation

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