5hq3

X-ray diffraction
2.6Å resolution

Stable, high-expression variant of human acetylcholinesterase

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 548 amino acids
Theoretical weight: 61.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: alpha/beta hydrolase
Acetylcholinesterase Chain: B
Molecule details ›
Chain: B
Length: 549 amino acids
Theoretical weight: 61.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P43212
Unit cell:
a: 89.534Å b: 89.534Å c: 395.305Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.253
Expression system: Escherichia coli