› 1xlu

X-ray diffraction
2.2Å resolution

X-Ray Structure Of Di-Isopropyl-Phosphoro-Fluoridate (Dfp) Inhibited Butyrylcholinesterase after Aging

Released:
DOI: 10.2210/pdb1xlu/pdb
PDB entry 1xlu coloured by chain, front view.
PDB entry 1xlu coloured by chain, side view.
PDB entry 1xlu 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 (3 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
Carbohydrate polymer
5 bound ligands:
Ligand NAG 3 x NAG
Ligand SO4 3 x SO4
Ligand CL 2 x CL
Ligand ISP 1 x ISP
Ligand GOL 4 x GOL
1 modified residue:
Ligand CSS 1 x CSS

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: I422
Unit cell:
a: 154.495Å b: 154.495Å c: 127.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.242
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

3 mentions without citation

Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking.
Juhl et al. (2009)
2 more