› 4pse

X-ray diffraction
1.71Å resolution

Trichoderma reesei cutinase in complex with a C11Y4 phosphonate inhibitor

Released:
DOI: 10.2210/pdb4pse/pdb
PDB entry 4pse coloured by chain, front view.
PDB entry 4pse coloured by chain, side view.
PDB entry 4pse coloured by chain, top view.
Source organism: Trichoderma reesei QM6a
Primary publication:
A Cutinase from Trichoderma reesei with a lid-covered active site and kinetic properties of true lipases.
Roussel A, Amara S, Nyyssölä A, Mateos-Diaz E, Blangy S, Kontkanen H, Westerholm-Parvinen A, Carrière F, Cambillau C
J Mol Biol 426 3757-3772 (2014)
PMID: 25219509

Function and Biology Details

Reaction catalysed: 
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-100128 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cutinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 254 amino acids
Theoretical weight: 26.77 KDa
Source organism: Trichoderma reesei QM6a
Expression system: Trichoderma reesei
UniProt:
  • Canonical: A0A024SC78 (Residues: 45-248; Coverage: 88%)
Gene name: M419DRAFT_76732
Sequence domains: Cutinase

Ligands and Environments

2 bound ligands:
Ligand C11 2 x C11
Ligand BOG 2 x BOG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 49.043Å b: 37.544Å c: 133.009Å
α: 90° β: 97.38° γ: 90°
R-values:
R R work R free
0.221 0.22 0.234
Expression system: Trichoderma reesei

Quick links

Citations

4 review citations

The Plant Polyester Cutin: Biosynthesis, Structure, and Biological Roles.
Fich et al. (2016)
3 more

3 mentions without citation

Comparative Structural Analysis of Different Mycobacteriophage-Derived Mycolylarabinogalactan Esterases (Lysin B).
Korany et al. (2019)
2 more