2IWI

CRYSTAL STRUCTURE OF THE HUMAN PIM2 IN COMPLEX WITH A RUTHENIUM ORGANOMETALLIC LIGAND RU1


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.242 
  • R-Value Observed: 0.244 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.6 of the entry. See complete history


Literature

Crystal structure of the PIM2 kinase in complex with an organoruthenium inhibitor.

Bullock, A.N.Russo, S.Amos, A.Pagano, N.Bregman, H.Debreczeni, J.E.Lee, W.H.von Delft, F.Meggers, E.Knapp, S.

(2009) PLoS One 4: e7112-e7112

  • DOI: https://doi.org/10.1371/journal.pone.0007112
  • Primary Citation of Related Structures:  
    2IWI

  • PubMed Abstract: 

    The serine/threonine kinase PIM2 is highly expressed in human leukemia and lymphomas and has been shown to positively regulate survival and proliferation of tumor cells. Its diverse ATP site makes PIM2 a promising target for the development of anticancer agents. To date our knowledge of catalytic domain structures of the PIM kinase family is limited to PIM1 which has been extensively studied and which shares about 50% sequence identity with PIM2.


  • Organizational Affiliation

    University of Oxford, Structural Genomics Consortium, Oxford, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SERINE/THREONINE-PROTEIN KINASE PIM-2
A, B
312Homo sapiensMutation(s): 0 
EC: 2.7.11.1
UniProt & NIH Common Fund Data Resources
Find proteins for Q9P1W9 (Homo sapiens)
Explore Q9P1W9 
Go to UniProtKB:  Q9P1W9
PHAROS:  Q9P1W9
GTEx:  ENSG00000102096 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9P1W9
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
HB1
Query on HB1

Download Ideal Coordinates CCD File 
C [auth A],
D [auth B]
RUTHENIUM-PYRIDOCARBAZOLE-1
C23 H13 N3 O3 Ru
HQDDSWVENMEGOZ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.80 Å
  • R-Value Free: 0.289 
  • R-Value Work: 0.242 
  • R-Value Observed: 0.244 
  • Space Group: H 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 153.07α = 90
b = 153.07β = 90
c = 78.6γ = 120
Software Package:
Software NamePurpose
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2006-08-02
    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: 2018-01-24
    Changes: Database references, Structure summary
  • Version 1.4: 2018-02-28
    Changes: Database references, Source and taxonomy
  • Version 1.5: 2019-05-08
    Changes: Data collection, Experimental preparation
  • Version 1.6: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description