3Q0V

ETHR From mycobacterium tuberculosis in complex with compound bdm31369


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.169 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 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.Leroux, F.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 EthR
A, B
236Mycobacterium tuberculosisMutation(s): 0 
Gene Names: ethRetaRMT3970Rv3855
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
LL4
Query on LL4

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
4-methyl-1-{4-[3-(thiophen-2-yl)-1,2,4-oxadiazol-5-yl]piperidin-1-yl}pentan-1-one
C17 H23 N3 O2 S
QWPAQBJBWLSPSH-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
LL4 BindingDB:  3Q0V IC50: 900 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.95 Å
  • R-Value Free: 0.228 
  • R-Value Work: 0.166 
  • R-Value Observed: 0.169 
  • Space Group: P 41
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 121.56α = 90
b = 121.56β = 90
c = 33.77γ = 90
Software Package:
Software NamePurpose
MOLREPphasing
REFMACrefinement
XDSdata reduction
XDSdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

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