› 6uqv

X-ray diffraction
1.35Å resolution

Crystal structure of ChoE, a bacterial acetylcholinesterase from Pseudomonas aeruginosa

Released:
DOI: 10.2210/pdb6uqv/pdb
PDB entry 6uqv coloured by chain, front view.
PDB entry 6uqv coloured by chain, side view.
PDB entry 6uqv coloured by chain, top view.
Source organism: Pseudomonas aeruginosa PAO1
Primary publication:
Structural insights into the putative bacterial acetylcholinesterase ChoE and its substrate inhibition mechanism.
Pham VD, To TA, Gagné-Thivierge C, Couture M, Lagüe P, Yao D, Picard MÈ, Lortie LA, Attéré SA, Zhu X, Levesque RC, Charette SJ, Shi R
J Biol Chem 295 8708-8724 (2020)
PMID: 32371400

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190970 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ChoE Chain: A
Molecule details ›
Chain: A
Length: 287 amino acids
Theoretical weight: 31.54 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9HUP2 (Residues: 21-307; Coverage: 100%)
Gene names: PA4921, choE
Sequence domains: GDSL-like Lipase/Acylhydrolase

Ligands and Environments

5 bound ligands:
Ligand MES 1 x MES
Ligand GOL 1 x GOL
Ligand BUA 1 x BUA
Ligand CL 1 x CL
Ligand P6G 1 x P6G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2221
Unit cell:
a: 82.157Å b: 109.673Å c: 84.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.154 0.177
Expression system: Escherichia coli BL21(DE3)

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Citations

2 citation in other articles

Biofilm formation as an extra gear for Apilactobacillus kunkeei to counter the threat of agrochemicals in honeybee crop.
Tlais et al. (2022)
1 more

3 mentions without citation

Structural insights into the putative bacterial acetylcholinesterase ChoE and its substrate inhibition mechanism.
Pham et al. (2020)
2 more