PDBe 1maa

X-ray diffraction
2.9Å resolution

MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 547 amino acids
Theoretical weight: 60.28 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-578; Coverage: 94%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: Rossmann fold

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 136.55Å b: 173.13Å c: 224.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.248
Expression system: Homo sapiens