1PAX

THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH 3,4-DIHYDRO-5-METHYL-ISOQUINOLINONE

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.169 
  • R-Value Observed: 0.169 

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This is version 1.3 of the entry. See complete history. 


Literature

Structure of the catalytic fragment of poly(ADP-ribose) polymerase from chicken.

Ruf, A., Mennissier de Murcia, J., de Murcia, G., Schulz, G.E.

(1996) Proc Natl Acad Sci U S A 93: 7481-7485

  • DOI: https://doi.org/10.1073/pnas.93.15.7481
  • Primary Citation of Related Structures:  
    1PAX

  • PubMed Abstract: 

    The crystal structures of the catalytic fragment of chicken poly(ADP-ribose) polymerase [NAD+ ADP-ribosyltransferase; NAD+:poly(adenosine-diphosphate-D-ribosyl)-acceptor ADP-D-ribosyltransferase, EC 2.4.2.30] with and without a nicotinamide-analogue inhibitor have been elucidated. Because this enzyme is involved in the regulation of DNA repair, its inhibitors are of interest for cancer therapy. The inhibitor shows the nicotinamide site and also suggests the adenosine site. The enzyme is structurally related to bacterial ADP-ribosylating toxins but contains an additional alpha-helical domain that is suggested to relay the activation signal issued on binding to damaged DNA.

    • Organizational Affiliation: 

    Institut für Organische Chemie und Biochemie, Freiburg im Breisgau, Germany.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
POLY(ADP-RIBOSE) POLYMERASE361Gallus gallusMutation(s): 0 
EC: 2.4.2.30 (PDB Primary Data), 2.4.2 (UniProt)
UniProt
Find proteins for P26446 (Gallus gallus)
Explore P26446 
Go to UniProtKB:  P26446
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP26446
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
DHQ
Query on DHQ
Download Ideal Coordinates CCD File 
B [auth A]3,4-DIHYDRO-5-METHYL-ISOQUINOLINONE
C10 H11 N O
RLLZPXDJYADIEU-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
DHQ BindingDB:  1PAX Ki: 70 (nM) from 1 assay(s)
IC50: min: 150, max: 420 (nM) from 3 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.244 
  • R-Value Work: 0.169 
  • R-Value Observed: 0.169 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 59.2α = 90
b = 64.5β = 90
c = 96.4γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
DENZOdata reduction
X-PLORphasing

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: 1997-05-15
    Type: Initial release
  • Version 1.1: 2008-03-04
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Derived calculations, Other