3Q0U

EthR from Mycobacterium tuberculosis in complex with compound BDM31379

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.202 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.2 of the entry. See complete history. 


Literature

Design, synthesis and optimization of new EthR inhibitors. A new alternative approach to fight tuberculosis by boosting ethionamide

Flipo, M., Desroses, M., Dirie, B., Carette, X., Lens, Z., Rucktooa, P., Leroux, F., Piveteau, C., Demirkaya, F., Locht, C., Villeret, V., Christophe, T., Jeon, H.K., Brodin, P., Deprez, B., Baulard, A., Willand, N.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
HTH-type transcriptional regulator EthR236Mycobacterium tuberculosisMutation(s): 0 
Gene Names: ethR, etaR, MT3970, Rv3855
UniProt
Find proteins for P9WMC1 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
Explore P9WMC1 
Go to UniProtKB:  P9WMC1
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP9WMC1
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LL3
Query on LL3
Download Ideal Coordinates CCD File 
B [auth A]2-phenyl-1-{4-[3-(thiophen-2-yl)-1,2,4-oxadiazol-5-yl]piperidin-1-yl}ethanone
C19 H19 N3 O2 S
FNAMKJFTCMWMKP-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
LL3 BindingDB:  3Q0U IC50: 5600 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.70 Å
  • R-Value Free: 0.234 
  • R-Value Work: 0.200 
  • R-Value Observed: 0.202 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 122.17α = 90
b = 122.17β = 90
c = 33.67γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-01-11
    Type: Initial release
  • Version 1.1: 2018-01-24
    Changes: Database references
  • Version 1.2: 2024-02-21
    Changes: Data collection, Database references, Derived calculations