› 7b38

X-ray diffraction
1.85Å resolution

Torpedo californica acetylcholinesterase complexed with Mg+2

Released:
DOI: 10.2210/pdb7b38/pdb
PDB entry 7b38 coloured by chain, front view.
PDB entry 7b38 coloured by chain, side view.
PDB entry 7b38 coloured by chain, top view.
Source organism: Tetronarce californica
Primary publication:
Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif.
Silman I, Shnyrov VL, Ashani Y, Roth E, Nicolas A, Sussman JL, Weiner L
Protein Sci 30 966-981 (2021)
PMID: 33686648

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
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

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
7 bound ligands:
Ligand MG 4 x MG
Ligand ZN 1 x ZN
Ligand NAG 2 x NAG
Ligand PGE 1 x PGE
Ligand GOL 3 x GOL
Ligand EDO 7 x EDO
Ligand PEG 2 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3221
Unit cell:
a: 138.217Å b: 138.217Å c: 71.376Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.202 0.241

Quick links

Citations

3 citation in other articles

GrAfSS: a webserver for substructure similarity searching and comparisons in the structures of proteins and RNA.
Ghani et al. (2022)
2 more

1 mention without citation

Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif.
Silman et al. (2021)