2whp

X-ray diffraction
2.2Å resolution

Crystal structure of acetylcholinesterase, phosphonylated by sarin and in complex with HI-6

Released:

Function and Biology Details

Reaction catalysed:
Acetylcholine + H(2)O = choline + acetate

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acetylcholinesterase Chain: A
Molecule details ›
Chain: A
Length: 548 amino acids
Theoretical weight: 60.35 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-576; Coverage: 94%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: Rossmann fold
Acetylcholinesterase Chain: B
Molecule details ›
Chain: B
Length: 548 amino acids
Theoretical weight: 60.34 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-576; Coverage: 94%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: Rossmann fold

Ligands and Environments


1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P212121
Unit cell:
a: 79.26Å b: 112.15Å c: 226.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.175 0.21
Expression system: Homo sapiens