2ack

X-ray diffraction
2.4Å resolution

ACETYLCHOLINESTERASE COMPLEXED WITH EDROPHONIUM, MONOCHROMATIC DATA

Released:
Source organism: Tetronarce californica
Primary publication:
Static Laue diffraction studies on acetylcholinesterase.
Acta Crystallogr. D Biol. Crystallogr. 54 1359-66 (1998)
PMID: 10089512

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (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: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P3121
Unit cell:
a: 112.409Å b: 112.409Å c: 136.55Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 not available 0.257