6HCO

Cryo-EM structure of the ABCG2 E211Q mutant bound to estrone 3-sulfate and 5D3-Fab


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.58 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation 3D Report Full Report


This is version 1.0 of the entry. See complete history

Literature

Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states

Manolaridis, I.Jackson, S.M.Taylor, N.M.I.Kowal, J.Stahlberg, H.Locher, K.P.

(2018) Nature --: --


Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
ATP-binding cassette sub-family G member 2
A, B
664Homo sapiensMutation(s): 1 
Gene Names: ABCG2 (ABCP, BCRP, BCRP1, MXR)
Find proteins for Q9UNQ0 (Homo sapiens)
Go to Gene View: ABCG2
Go to UniProtKB:  Q9UNQ0
Entity ID: 2
MoleculeChainsSequence LengthOrganismDetails
5D3-Fab light chain
C, E
214N/AMutation(s): 0 
Protein Feature View is not available: No corresponding UniProt sequence found.
Entity ID: 3
MoleculeChainsSequence LengthOrganismDetails
5D3-Fab heavy chain
D, F
221N/AMutation(s): 0 
Protein Feature View is not available: No corresponding UniProt sequence found.
Small Molecules
Ligands 2 Unique
IDChainsName / Formula / InChI Key2D Diagram3D Interactions
FY5
Query on FY5

Download SDF File 
Download CCD File 
A
estrone 3-sulfate
C18 H22 O5 S
JKKFKPJIXZFSSB-OVWQWFNUSA-N
 Ligand Interaction
NAG
Query on NAG

Download SDF File 
Download CCD File 
A, B
N-ACETYL-D-GLUCOSAMINE
C8 H15 N O6
OVRNDRQMDRJTHS-FMDGEEDCSA-N
 Ligand Interaction
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.58 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
Software Package:
Software NamePurpose
PHENIXrefinement

Structure Validation

View Full Validation Report or Ramachandran Plots



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swiss National Science FoundationSwitzerland--
SwitzerlandETH-22-14-1

Revision History 

  • Version 1.0: 2018-11-07
    Type: Initial release