› 1jjb

X-ray diffraction
2.3Å resolution

A neutral molecule in cation-binding site: Specific binding of PEG-SH to Acetylcholinesterase from Torpedo californica

Released:
DOI: 10.2210/pdb1jjb/pdb
PDB entry 1jjb coloured by chain, front view.
PDB entry 1jjb coloured by chain, side view.
PDB entry 1jjb coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
A neutral molecule in a cation-binding site: specific binding of a PEG-SH to acetylcholinesterase from Torpedo californica.
Koellner G, Steiner T, Millard CB, Silman I, Sussman JL
J Mol Biol 320 721-5 (2002)
PMID: 12095250

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: 532 amino acids
Theoretical weight: 60.19 KDa
Source organism: Tetronarce californica
UniProt:
  • Canonical: P04058 (Residues: 25-556; Coverage: 94%)
Gene name: ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand NAG 2 x NAG
Ligand PE7 1 x PE7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P3121
Unit cell:
a: 111.2Å b: 111.2Å c: 137.119Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.178 0.224

Quick links

Citations

2 review citations

Cholinesterases, a target of pharmacology and toxicology.
Pohanka M. (2011)
1 more

3 mentions without citation

Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics.
Xu et al. (2008)
2 more