5luj

X-ray diffraction
2.2Å resolution

Structure of cutinase 2 from Thermobifida cellulosilytica

Released:

Function and Biology Details

Reactions catalysed:
(Ethylene terephthalate)(n) + H(2)O = (ethylene terephthalate)(n-1) + ethylene terephthalate
Cutin + H(2)O = cutin monomers
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123178 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cutinase 2 Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 28.87 KDa
Source organism: Thermobifida cellulosilytica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E9LVH9 (Residues: 1-262; Coverage: 100%)
Gene name: cut2
Sequence domains: Platelet-activating factor acetylhydrolase, isoform II
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Unit cell:
a: 36.67Å b: 43.15Å c: 152.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.241
Expression system: Escherichia coli BL21(DE3)