› 1xlw

X-ray diffraction
2.1Å resolution

Diethylphosphorylated Butyrylcholinesterase (Nonaged) Obtained By Reaction With Echothiophate

Released:
DOI: 10.2210/pdb1xlw/pdb
PDB entry 1xlw coloured by chain, front view.
PDB entry 1xlw coloured by chain, side view.
PDB entry 1xlw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging.
Nachon F, Asojo OA, Borgstahl GE, Masson P, Lockridge O
Biochemistry 44 1154-62 (2005)
PMID: 15667209

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138982 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Cholinesterase Chain: A
Molecule details ›
Chain: A
Length: 529 amino acids
Theoretical weight: 59.75 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
  • Canonical: P06276 (Residues: 29-557; 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
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
5 bound ligands:
Ligand NAG 3 x NAG
Ligand SO4 4 x SO4
Ligand CL 2 x CL
Ligand DEP 1 x DEP
Ligand GOL 3 x GOL
1 modified residue:
Ligand CSS 1 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I422
Unit cell:
a: 154.463Å b: 154.463Å c: 127.011Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.184 0.223
Expression system: Cricetulus griseus

Quick links

Citations

10 review citations

Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration.
Ekici et al. (2008)
9 more

11 mentions without citation

Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase.
Ngamelue et al. (2007)
10 more