› 7w1n

X-ray diffraction
1.88Å resolution

Complex structure of a leaf-branch compost cutinase variant LCC ICCG_KRP

Released:
DOI: 10.2210/pdb7w1n/pdb
PDB entry 7w1n coloured by chain, front view.
PDB entry 7w1n coloured by chain, side view.
PDB entry 7w1n coloured by chain, top view.
Source organism: unidentified prokaryotic organism
Primary publication:
Substrate-Binding Mode of a Thermophilic PET Hydrolase and Engineering the Enzyme to Enhance the Hydrolytic Efficacy.
Zeng W, Li X, Yang Y, Min J, Huang J-W, Liu W, Niu D, Yang X, Han X, Zhang L, Dai L, Chen C-C, Guo R-T
ACS Catalysis 12 3033-3040 (2022)

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124660 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leaf-branch compost cutinase Chain: A
Molecule details ›
Chain: A
Length: 270 amino acids
Theoretical weight: 28.59 KDa
Source organism: unidentified prokaryotic organism
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G9BY57 (Residues: 36-293; Coverage: 100%)
Sequence domains: Alpha/beta hydrolase family

Ligands and Environments

2 bound ligands:
Ligand BCN 1 x BCN
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER METALJET
Spacegroup: P212121
Unit cell:
a: 46.307Å b: 60.442Å c: 81.947Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.139 0.137 0.165
Expression system: Escherichia coli BL21(DE3)

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