2E9U

Structure of h-CHK1 complexed with A780125

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.277 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.242 

wwPDB Validation   3D Report Full Report


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


Literature

Structure-Based Design, Synthesis and Biological Evaluation of Potent Selective Macrocyclic Chk1 Inhibitors

Tong, Y., Claiborne, A., Stewart, K.D., Park, C., Kovar, P., Chen, Z., Credo, R.B., Gwaltney, S.L., Zhang, H., Rosenberg, S.H., Sham, H.L., Sowin, T.J., Lin, N.H.

To be published.

Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Serine/threonine-protein kinase Chk1269Homo sapiensMutation(s): 0 
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for O14757 (Homo sapiens)
Explore O14757 
Go to UniProtKB:  O14757
PHAROS:  O14757
GTEx:  ENSG00000149554 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO14757
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
A25
Query on A25
Download Ideal Coordinates CCD File 
B [auth A]18-CHLORO-11,12,13,14-TETRAHYDRO-1H,10H-8,4-(AZENO)-9,15,1,3,6-BENZODIOXATRIAZACYCLOHEPTADECIN-2-ONE
C16 H17 Cl N4 O3
JRSWWYITYIOHOP-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
A25 PDBBind:  2E9U Ki: 7.94 (nM) from 1 assay(s)
BindingDB:  2E9U Ki: 7.9 (nM) from 1 assay(s)
IC50: 10 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.277 
  • R-Value Work: 0.227 
  • R-Value Observed: 0.242 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.075α = 90
b = 65.82β = 94.37
c = 57.945γ = 90
Software Package:
Software NamePurpose
CNXrefinement
ADSCdata collection
HKL-2000data reduction
HKL-2000data scaling
CNSphasing

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

  • Released Date: 2008-01-29 
    • Deposition Author(s): Park, C.

Revision History  (Full details and data files)

  • Version 1.0: 2008-01-29
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2024-03-13
    Changes: Data collection, Database references, Derived calculations