› 1vot

X-ray diffraction
2.5Å resolution

ACETYLCHOLINESTERASE (E.C. 3.1.1.7) COMPLEXED WITH HUPERZINE A

Released:
DOI: 10.2210/pdb1vot/pdb
PDB entry 1vot coloured by chain, front view.
PDB entry 1vot coloured by chain, side view.
PDB entry 1vot coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A.
Raves ML, Harel M, Pang YP, Silman I, Kozikowski AP, Sussman JL
Nat Struct Biol 4 57-63 (1997)
PMID: 8989325

Function and Biology Details

Reaction catalysed: 
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 537 amino acids
Theoretical weight: 60.74 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 22-558; Coverage: 95%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand HUP 1 x HUP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P3121
Unit cell:
a: 112.632Å b: 112.632Å c: 136.378Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.205 0.248

Quick links

Citations

28 review citations

Implications of protein flexibility for drug discovery.
Teague SJ. (2003)
27 more

12 mentions without citation

Molecular dynamics simulations: advances and applications.
Hospital et al. (2015)
11 more