› 3dd5

X-ray diffraction
2.6Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-145806 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cutinase 1 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 201 amino acids
Theoretical weight: 21.09 KDa
Source organism: Colletotrichum gloeosporioides
Expression system: Escherichia coli
UniProt:
  • Canonical: P11373 (Residues: 31-224; Coverage: 93%)
Gene name: CUTA
Sequence domains: Cutinase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand DEP 8 x DEP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 73.47Å b: 117.37Å c: 95.24Å
α: 90° β: 103.57° γ: 90°
R-values:
R R work R free
0.219 0.215 0.279
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

2 mentions without citation

Mycobacteriophage Lysin B is a novel mycolylarabinogalactan esterase.
Payne et al. (2009)
1 more