5NXD

LIM Domain Kinase 2 (LIMK2) In Complex With TH-300


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.197 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

LIM Domain Kinase 2 (LIMK2)In Complex With TH-300

Mathea, S.Salah, E.Hanke, T.Newman, J.A.Oerum, S.Wang, D.Burgess-Brown, N.von Delft, F.Arrowsmith, C.H.Edwards, A.M.Bountra, C.Bullock, A.N.Knapp, S.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LIM domain kinase 2
A, B
305Homo sapiensMutation(s): 0 
Gene Names: LIMK2
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for P53671 (Homo sapiens)
Explore P53671 
Go to UniProtKB:  P53671
PHAROS:  P53671
GTEx:  ENSG00000182541 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP53671
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.230 
  • R-Value Work: 0.195 
  • R-Value Observed: 0.197 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 63.275α = 90
b = 66.605β = 97.43
c = 82.124γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
xia2data reduction
xia2data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2017-05-24
    Type: Initial release
  • Version 1.1: 2024-01-17
    Changes: Data collection, Database references, Refinement description