4U6A | pdb_00004u6a

X-ray crystal structure of human TNKS in complex with a small molecule inhibitor


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.37 Å
  • R-Value Free: 
    0.248 (Depositor), 0.270 (DCC) 
  • R-Value Work: 
    0.191 (Depositor), 0.200 (DCC) 
  • R-Value Observed: 
    0.194 (Depositor) 

Starting Model: experimental
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wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted 3DNClick on this verticalbar to view details

This is version 1.2 of the entry. See complete history


Literature

Design and discovery of 3-aryl-5-substituted-isoquinolin-1- ones as potent and selective tankyrase inhibitors

Elliot, R.J.Jarvis, A.Rajasekaran, M.B.Menon, M.Bowers, L.Boffey, R.Bayford, M.Firth-Clark, S.Beevers, R.Aquil, R.Kirton, S.B.Niculescu-Duvaz, D.Fish, L.Lopes, F.McLeary, R.Trindade, I.Vendrell, E.Munkonge, F.Porter, R.Perrior, T.Springer, C.Oliver, A.W.Pearl, L.H.Ashworth, A.Lord, C.J.

To be published.

Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Tankyrase-1258Homo sapiensMutation(s): 1 
Gene Names: TNKSPARP5APARPLTIN1TINF1TNKS1
EC: 2.4.2.30 (PDB Primary Data), 2.4.2 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for O95271 (Homo sapiens)
Explore O95271 
Go to UniProtKB:  O95271
PHAROS:  O95271
GTEx:  ENSG00000173273 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO95271
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
3DN
Query on 3DN

Download Ideal Coordinates CCD File 
C [auth A]3-(4-{[4-(dimethylamino)piperidin-1-yl]methyl}phenyl)-5-methylisoquinolin-1(2H)-one
C24 H29 N3 O
ZAVBKFISCRSHAT-UHFFFAOYSA-N
GOL
Query on GOL

Download Ideal Coordinates CCD File 
D [auth A],
E [auth A],
F [auth A],
H [auth A],
J [auth A]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN
Query on ZN

Download Ideal Coordinates CCD File 
B [auth A]ZINC ION
Zn
PTFCDOFLOPIGGS-UHFFFAOYSA-N
EDO
Query on EDO

Download Ideal Coordinates CCD File 
G [auth A],
I [auth A]
1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.37 Å
  • R-Value Free:  0.248 (Depositor), 0.270 (DCC) 
  • R-Value Work:  0.191 (Depositor), 0.200 (DCC) 
  • R-Value Observed: 0.194 (Depositor) 
Space Group: I 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 81.38α = 90
b = 80.98β = 90
c = 84.02γ = 90
Software Package:
Software NamePurpose
BUSTERrefinement
XDSdata reduction
Aimlessdata scaling
PDB_EXTRACTdata extraction
PHASERphasing
XSCALEdata reduction
XSCALEdata scaling

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 

Created with Raphaël 2.3.0Worse 01 BetterLigand structure goodness of fit to experimental dataBest fitted 3DNClick on this verticalbar to view details

Entry History & Funding Information

Deposition Data

  • Released Date: 2015-07-08 
  • Deposition Author(s): Oliver, A.W.

Funding OrganizationLocationGrant Number
Wellcome TrustUnited KingdomSDDI

Revision History  (Full details and data files)

  • Version 1.0: 2015-07-08
    Type: Initial release
  • Version 1.1: 2015-07-15
    Changes: Other
  • Version 1.2: 2023-12-20
    Changes: Data collection, Database references, Derived calculations, Refinement description