› 6i2t

Electron Microscopy
5.7Å resolution

CryoEM reconstruction of full-length, fully-glycosylated human butyrylcholinesterase tetramer

Released:
DOI: 10.2210/pdb6i2t/pdb
PDB entry 6i2t coloured by chain, front view.
PDB entry 6i2t coloured by chain, side view.
PDB entry 6i2t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cryo-EM structure of the native butyrylcholinesterase tetramer reveals a dimer of dimers stabilized by a superhelical assembly.
Leung MR, van Bezouwen LS, Schopfer LM, Sussman JL, Silman I, Lockridge O, Zeev-Ben-Mordehai T
Proc Natl Acad Sci U S A 115 13270-13275 (2018)
PMID: 30538207
Related structures: EMD-4400

Function and Biology Details

Reaction catalysed: 
An acylcholine + H(2)O = choline + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138985 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cholinesterase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 574 amino acids
Theoretical weight: 65.15 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P06276 (Residues: 29-602; Coverage: 100%)
Gene names: BCHE, CHE1
Sequence domains:
lamellipodin-derived polyproline peptide Chain: J
Molecule details ›
Chain: J
Length: 12 amino acids
Theoretical weight: 1.18 KDa
Source organism: Homo sapiens

Ligands and Environments

1 bound ligand:
Ligand NAG 8 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 5.7Å
Relevant EMDB volumes: EMD-4400

Quick links

Citations

3 review citations

A Comprehensive Review of Cholinesterase Modeling and Simulation.
De Boer et al. (2021)
2 more

5 mentions without citation

Cryo-electron microscopy of cholinesterases, present and future.
Leung et al. (2021)
4 more