› 2xqi

X-ray diffraction
2.6Å resolution

X-ray Structure of human butyrylcholinesterase inhibited by racemic CVX

Released:
DOI: 10.2210/pdb2xqi/pdb
PDB entry 2xqi coloured by chain, front view.
PDB entry 2xqi coloured by chain, side view.
PDB entry 2xqi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural study of the complex stereoselectivity of human butyrylcholinesterase for the neurotoxic V-agents.
Wandhammer M, Carletti E, Van der Schans M, Gillon E, Nicolet Y, Masson P, Goeldner M, Noort D, Nachon F
J Biol Chem 286 16783-9 (2011)
PMID: 21454498

Function and Biology Details

Reaction catalysed: 
An acylcholine + H(2)O = choline + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138986 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Cholinesterase Chain: A
Molecule details ›
Chain: A
Length: 527 amino acids
Theoretical weight: 59.47 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P06276 (Residues: 31-557; Coverage: 92%)
Gene names: BCHE, CHE1
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUL
Carbohydrate polymer
7 bound ligands:
Ligand GLY 1 x GLY
Ligand CVX 1 x CVX
Ligand CL 3 x CL
Ligand NA 3 x NA
Ligand SO4 2 x SO4
Ligand NAG 4 x NAG
Ligand UNX 25 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I422
Unit cell:
a: 155.15Å b: 155.15Å c: 128.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.247
Expression system: Cricetulus griseus

Quick links

Citations

3 review citations

Progress in the development of enzyme-based nerve agent bioscavengers.
Nachon et al. (2013)
2 more

1 mention without citation

Structural study of the complex stereoselectivity of human butyrylcholinesterase for the neurotoxic V-agents.
Wandhammer et al. (2011)