4HOK

crystal structure of apo ck1e


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.77 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.241 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Structural basis for the potent and selective inhibition of casein kinase 1 epsilon.

Long, A.M.Zhao, H.Huang, X.

(2012) J Med Chem 55: 10307-10311

  • DOI: https://doi.org/10.1021/jm301336n
  • Primary Citation of Related Structures:  
    4HNF, 4HNI, 4HOK

  • PubMed Abstract: 

    Casein kinase 1 epsilon (CK1ε) and its closest homologue CK1δ are key regulators of diverse cellular processes. We report two crystal structures of PF4800567, a potent and selective inhibitor of CK1ε, bound to the kinase domains of human CK1ε and CK1δ as well as one apo CK1ε crystal structure. These structures provide a molecular basis for the strong and specific inhibitor interactions with CK1ε and suggest clues for further development of CK1δ inhibitors.


  • Organizational Affiliation

    Department of Molecular Structure and Characterization, Amgen Inc., 360 Binney Street, Cambridge, Massachusetts 02142, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Casein kinase I isoform epsilon296Homo sapiensMutation(s): 0 
Gene Names: CSNK1E
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for P49674 (Homo sapiens)
Explore P49674 
Go to UniProtKB:  P49674
PHAROS:  P49674
GTEx:  ENSG00000213923 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP49674
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

Download Ideal Coordinates CCD File 
M [auth A]
N [auth C]
O [auth E]
P [auth G]
Q [auth I]
M [auth A],
N [auth C],
O [auth E],
P [auth G],
Q [auth I],
R [auth K],
S [auth M],
T [auth O],
U [auth Q],
V [auth S],
W [auth U],
X [auth W]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.77 Å
  • R-Value Free: 0.262 
  • R-Value Work: 0.241 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 180.361α = 90
b = 142.496β = 108.57
c = 232.462γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHASESphasing
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2012-11-14
    Type: Initial release
  • Version 1.1: 2013-01-02
    Changes: Database references
  • Version 1.2: 2018-11-07
    Changes: Data collection, Experimental preparation
  • Version 1.3: 2024-02-28
    Changes: Data collection, Database references, Derived calculations