› 3vis

X-ray diffraction
1.76Å resolution

Crystal structure of cutinase Est119 from Thermobifida alba AHK119

Released:
DOI: 10.2210/pdb3vis/pdb
PDB entry 3vis coloured by chain, front view.
PDB entry 3vis coloured by chain, side view.
PDB entry 3vis coloured by chain, top view.
Source organism: Thermobifida alba
Primary publication:
Crystal structure of cutinase Est119 from Thermobida alba AHK119 that can degrade modpolyethylene terephthalate at 1.76 A resolution.
Kitadokoro K, Thumarat U, Nakamura R, Nishimura K, Karatani H, Suzuki H, Kawai F
Polym. Degrad. Stab. 97 771-775 (2012)

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123667 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cutinase est2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 306 amino acids
Theoretical weight: 33.22 KDa
Source organism: Thermobifida alba
Expression system: Escherichia coli
UniProt:
  • Canonical: F7IX06 (Residues: 1-300; Coverage: 100%)
Gene names: est119, est2
Sequence domains: Platelet-activating factor acetylhydrolase, isoform II
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand PE4 1 x PE4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: C2
Unit cell:
a: 100.989Å b: 88.732Å c: 71.794Å
α: 90° β: 133.03° γ: 90°
R-values:
R R work R free
0.152 0.15 0.196
Expression system: Escherichia coli

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