› 5ehq

X-ray diffraction
2.5Å resolution

mAChE-anti TZ2PA5 complex

Released:
DOI: 10.2210/pdb5ehq/pdb
PDB entry 5ehq coloured by chain, front view.
PDB entry 5ehq coloured by chain, side view.
PDB entry 5ehq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Steric and Dynamic Parameters Influencing In Situ Cycloadditions to Form Triazole Inhibitors with Crystalline Acetylcholinesterase.
Bourne Y, Sharpless KB, Taylor P, Marchot P
J Am Chem Soc 138 1611-21 (2016)
PMID: 26731630

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-149441 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 543 amino acids
Theoretical weight: 59.76 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-574; Coverage: 93%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
3 bound ligands:
Ligand NAG 2 x NAG
Ligand 5O2 2 x 5O2
Ligand P6G 1 x P6G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 79.82Å b: 113.16Å c: 225.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 0.215
Expression system: Homo sapiens

Quick links

Citations

2 review citations

Protein-Templated Fragment Ligations-From Molecular Recognition to Drug Discovery.
Jaegle et al. (2017)
1 more