6o69

X-ray diffraction
2.08Å resolution

Crystal Structure of Double Mutant L380R/F535K of Human Acetylcholinesterase

Released:

Function and Biology Details

Reaction catalysed:
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 542 amino acids
Theoretical weight: 59.47 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P22303 (Residues: 33-574; Coverage: 93%)
Gene name: ACHE
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6522
Unit cell:
a: 115.783Å b: 115.783Å c: 191.859Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.186 0.222
Expression system: Homo sapiens