EMD-4400

Single-particle
5.7 Å
EMD-4400
3D View Gallery
Deposition: 01/11/2018
Map released: 19/12/2018
Last modified: 13/11/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-4400

Archive Files (Depositor)

Primary 3D volume (map.gz) Experimental metadata (xml) Experimental metadata (cif.gz)

Validation (wwPDB)

Map-only validation report (pdf.gz) Map-6i2t summary report (pdf.gz) Map-6i2t FULL report (pdf.gz)

EMDB Annotations

EMICSS entry mapping (xml)

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

EMD-4400

Single-particle
5.7 Å
EMD-4400
3D View Gallery
Deposition: 01/11/2018
Map released: 19/12/2018
Last modified: 13/11/2024
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Homo sapiens
Sample: heteropentameric complex consisting of four copies of butyrylcholinesterase and one copy of a lamellipodin-derived polyproline peptide
Fitted models: 6i2t

Deposition Authors: Leung MR , van Bezouwen LS
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
(2018) PNAS , 115 , 13270 - 13275
PUBMED: 30538207
DOI: doi:10.1073/pnas.1817009115
ISSN: 1091-6490
ASTM: PNASA6