4cg3

X-ray diffraction
1.55Å resolution

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

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-179387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cutinase cut2 Chain: A
Molecule details ›
Chain: A
Length: 313 amino acids
Theoretical weight: 33.79 KDa
Source organism: Thermobifida fusca
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6A0I4 (Residues: 41-301; Coverage: 100%)
Gene names: TfH, bta1, cut1, cut2
Sequence domains: Chlorophyllase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: I41
Unit cell:
a: 117.9Å b: 117.9Å c: 36.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.12 0.117 0.149
Expression system: Escherichia coli