7NDV

X-ray structure of acetylcholine-binding protein (AChBP) in complex with FL001888.


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.233 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.206 

wwPDB Validation   3D Report Full Report


This is version 1.0 of the entry. See complete history


Literature

Discovery of fragments inducing conformational effects in dynamic proteins using a second-harmonic generation biosensor

Fitzgerald, E.A.Butko, M.T.Boronat, P.Cederfelt, D.Abramsson, M.Ludviksdottir, H.van Muijlwijk-Koezen, J.de Esch, I.J.P.Dobritzsch, D.Young, T.Danielson, U.H.

(2021) Rsc Advances 11: 7527-7537


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  Structure
Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
Acetylcholine-binding proteinABCDEFGHABCDEFGHIJ
237Lymnaea stagnalisMutation(s): 0 
Find proteins for P58154 (Lymnaea stagnalis)
Explore P58154 
Go to UniProtKB:  P58154
Protein Feature View
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.233 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.206 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 76.68α = 90
b = 121.27β = 90
c = 239.3γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PHASERphasing
XSCALEdata scaling
XDSdata reduction

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Marie Sklodowska-Curie Actions, FragNET ITNEuropean Union675899

Revision History  (Full details and data files)

  • Version 1.0: 2021-04-07
    Type: Initial release