› 2c5f

X-ray diffraction
2.6Å resolution

Torpedo californica acetylcholinesterase in complex with a non hydrolysable substrate analogue, 4-oxo-N,N,N-trimethylpentanaminium

Released:
DOI: 10.2210/pdb2c5f/pdb
PDB entry 2c5f coloured by chain, front view.
PDB entry 2c5f coloured by chain, side view.
PDB entry 2c5f coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Structural insights into substrate traffic and inhibition in acetylcholinesterase.
Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman JL, Zaccai G, Silman I, Weik M
EMBO J 25 2746-56 (2006)
PMID: 16763558

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

4 bound ligands:
Ligand NAG 2 x NAG
Ligand PGE 3 x PGE
Ligand NWA 1 x NWA
Ligand CHH 1 x CHH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P3121
Unit cell:
a: 112.26Å b: 112.26Å c: 137Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.163 0.163 0.22

Quick links

Citations

8 review citations

The biological significance of substrate inhibition: a mechanism with diverse functions.
Reed et al. (2010)
7 more

9 mentions without citation

Mining electron density for functionally relevant protein polysterism in crystal structures.
Fraser et al. (2011)
8 more