X-ray diffraction
1.44Å resolution

Structural and functional studies on a thermostable polyethylene terephthalate degrading hydrolase from Thermobifida fusca


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Cutinase cut2 Chain: A
Molecule details ›
Chain: A
Length: 282 amino acids
Theoretical weight: 30.64 KDa
Source organism: Thermobifida fusca
Expression system: Escherichia coli
  • Canonical: Q6A0I4 (Residues: 41-301; Coverage: 100%)
Gene names: TfH, bta1, cut1, cut2
Sequence domains: Chlorophyllase enzyme
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: I41
Unit cell:
a: 116.591Å b: 116.591Å c: 35.581Å
α: 90° β: 90° γ: 90°
R R work R free
0.141 0.138 0.166
Expression system: Escherichia coli