2JED

The crystal structure of the kinase domain of the protein kinase C theta in complex with NVP-XAA228 at 2.32A resolution.

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.32 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 

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Ligand Structure Quality Assessment 


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


Literature

The Crystal Structure of the Kinase Domain of the Protein Kinase C Theta in Complex with Nvp-Xaa228

Stark, W., Bitsch, F., Berner, A., Buelens, F., Graff, P., Depersin, H., Fendrich, G., Geiser, M., Knecht, R., Rahuel, J., Rummel, G., Schlaeppi, J.M., Schmitz, R., Strauss, A., Wagner, J.

To be published.

Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN KINASE C THETA
A, B
352Homo sapiensMutation(s): 2 
EC: 2.7.11.13
UniProt & NIH Common Fund Data Resources
Find proteins for Q04759 (Homo sapiens)
Explore Q04759 
Go to UniProtKB:  Q04759
PHAROS:  Q04759
GTEx:  ENSG00000065675 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ04759
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
LG8
Query on LG8
Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]		3-(8-DIMETHYLAMINOMETHYL-6,7,8,9-TETRAHYDRO-PYRIDO[1,2-A]INDOL-10-YL)-4-(1-METHYL-1H-INDOL-3-YL)-PYRROLE-2,5-DIONE
C28 H28 N4 O2
OYDDKWPGAIBVKO-JQQWWDHGSA-O
MPD
Query on MPD
Download Ideal Coordinates CCD File 
E [auth B](4S)-2-METHYL-2,4-PENTANEDIOL
C6 H14 O2
SVTBMSDMJJWYQN-YFKPBYRVSA-N
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
SEP
Query on SEP
A, B
L-PEPTIDE LINKINGC3 H8 N O6 PSER
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.32 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.186 
  • R-Value Observed: 0.188 
  • Space Group: P 65
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 152.172α = 90
b = 152.172β = 90
c = 74.837γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing

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: 2008-02-05
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2019-05-15
    Changes: Data collection, Derived calculations, Experimental preparation, Other
  • Version 1.4: 2019-09-25
    Changes: Data collection, Experimental preparation, Other
  • Version 1.5: 2023-12-13
    Changes: Data collection, Database references, Refinement description