2WEI

Crystal structure of the kinase domain of Cryptosporidium parvum calcium dependent protein kinase in complex with 3-MB-PP1

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.197 

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This is version 1.5 of the entry. See complete history. 


Literature

The Cryptosporidium Parvum Kinome.

Artz, J.D., Wernimont, A.K., Allali-Hassani, A., Zhao, Y., Amani, M., Lin, Y.H., Senisterra, G., Wasney, G.A., Fedorov, O., King, O., Roos, A.K., Lunin, V.V., Qiu, W., Finerty, P.J., Hutchinson, A., Chau, I., von Delft, F., MacKenzie, F.I., Lew, J., Kozieradzki, I., Vedadi, M., Schapira, M., Zhang, C., Shokat, K.M., Heightman, T., Hui, R.

(2011) BMC Genomics 12: 478

  • DOI: https://doi.org/10.1186/1471-2164-12-478
  • Primary Citation of Related Structures:  
    2WEI

  • PubMed Abstract: 

    Hundreds of millions of people are infected with cryptosporidiosis annually, with immunocompromised individuals suffering debilitating symptoms and children in socioeconomically challenged regions at risk of repeated infections. There is currently no effective drug available. In order to facilitate the pursuit of anti-cryptosporidiosis targets and compounds, our study spans the classification of the Cryptosporidium parvum kinome and the structural and biochemical characterization of representatives from the CDPK family and a MAP kinase.

    • Organizational Affiliation: 

    Structural Genomics Consortium, University of Toronto, MaRS South Tower, Floor 7, 101 College St, Toronto, Ontario M5G 1L7, Canada. jdartz@gmail.com


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
CALMODULIN-DOMAIN PROTEIN KINASE 1, PUTATIVE287Cryptosporidium parvum Iowa IIMutation(s): 0 
Gene Names: CGD3_920
EC: 2.7.1.17
UniProt
Find proteins for A3FQ16 (Cryptosporidium parvum (strain Iowa II))
Explore A3FQ16 
Go to UniProtKB:  A3FQ16
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA3FQ16
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
VGG
Query on VGG
Download Ideal Coordinates CCD File 
B [auth A]1-tert-butyl-3-(3-methylbenzyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine
C17 H21 N5
FYCOTGCSHZKHPR-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
VGG Binding MOAD:  2WEI IC50: 3.4 (nM) from 1 assay(s)
PDBBind:  2WEI IC50: 3.4 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.65 Å
  • R-Value Free: 0.229 
  • R-Value Work: 0.196 
  • R-Value Observed: 0.197 
  • Space Group: P 43 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 68.9α = 90
b = 68.9β = 90
c = 130.46γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

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Ligand Structure Quality Assessment 


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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2009-04-28
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 1.2: 2011-10-12
    Changes: Database references, Derived calculations, Refinement description
  • Version 1.3: 2012-12-05
    Changes: Database references, Structure summary
  • Version 1.4: 2018-01-24
    Changes: Database references, Structure summary
  • Version 1.5: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description