4E20

Structure of mouse Tyk-2 complexed to a 3-aminoindazole inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.233 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.200 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Enabling structure-based drug design of Tyk2 through co-crystallization with a stabilizing aminoindazole inhibitor.

Argiriadi, M.A.Goedken, E.R.Banach, D.Borhani, D.W.Burchat, A.Dixon, R.W.Marcotte, D.Overmeyer, G.Pivorunas, V.Sadhukhan, R.Sousa, S.Moore, N.S.Tomlinson, M.Voss, J.Wang, L.Wishart, N.Woller, K.Talanian, R.V.

(2012) BMC Struct Biol 12: 22-22

  • DOI: https://doi.org/10.1186/1472-6807-12-22
  • Primary Citation of Related Structures:  
    4E1Z, 4E20

  • PubMed Abstract: 

    Structure-based drug design (SBDD) can accelerate inhibitor lead design and optimization, and efficient methods including protein purification, characterization, crystallization, and high-resolution diffraction are all needed for rapid, iterative structure determination. Janus kinases are important targets that are amenable to structure-based drug design. Here we present the first mouse Tyk2 crystal structures, which are complexed to 3-aminoindazole compounds.


  • Organizational Affiliation

    Department of Molecular & Cellular Pharmacology, Abbott Laboratories, Worcester, MA, USA. maria.argiriadi@abbott.com


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Non-receptor tyrosine-protein kinase TYK2290Mus musculusMutation(s): 1 
Gene Names: Tyk2
EC: 2.7.10.2
UniProt & NIH Common Fund Data Resources
Find proteins for Q9R117 (Mus musculus)
Explore Q9R117 
Go to UniProtKB:  Q9R117
IMPC:  MGI:1929470
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9R117
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
0MY
Query on 0MY

Download Ideal Coordinates CCD File 
B [auth A]N-[4-(3-amino-1H-indazol-5-yl)phenyl]-3-chlorobenzenesulfonamide
C19 H15 Cl N4 O2 S
AZLVHYHHBLHABI-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.233 
  • R-Value Work: 0.199 
  • R-Value Observed: 0.200 
  • Space Group: P 31 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 67.28α = 90
b = 67.28β = 90
c = 154.912γ = 120
Software Package:
Software NamePurpose
HKL-2000data collection
PHASERphasing
BUSTERrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-10-03
    Type: Initial release
  • Version 1.1: 2024-02-28
    Changes: Data collection, Database references, Derived calculations