› 8jmp

X-ray diffraction
1.9Å resolution

Structure of a leaf-branch compost cutinase, ICCG in complex with 1,4-butanediol terephthalate

Released:
DOI: 10.2210/pdb8jmp/pdb
PDB entry 8jmp coloured by chain, front view.
PDB entry 8jmp coloured by chain, side view.
PDB entry 8jmp coloured by chain, top view.
Source organism: unidentified prokaryotic organism
Primary publication:
Remodeling the polymer-binding cavity to improve the efficacy of PBAT-degrading enzyme.
Yang Y, Cheng S, Zheng Y, Xue T, Huang JW, Zhang L, Yang Y, Guo RT, Chen CC
J Hazard Mater 464 132965 (2023)
PMID: 37979420

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-124660 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leaf-branch compost cutinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 27.84 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 CA 1 x CA
Ligand EMX 1 x EMX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER METALJET
Spacegroup: P212121
Unit cell:
a: 41.19Å b: 84.928Å c: 147.979Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.154 0.196
Expression system: Escherichia coli BL21(DE3)

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