2Y37

The discovery of novel, potent and highly selective inhibitors of inducible nitric oxide synthase (iNOS)


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.208 
  • R-Value Observed: 0.210 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

The Discovery of Novel, Potent and Highly Selective Inhibitors of Inducible Nitric Oxide Synthase (Inos).

Cheshire, D.R.Berg, A.Andersson, G.M.Andrews, G.Beaton, H.G.Birkinshaw, T.N.Boughton-Smith, N.Connolly, S.Cook, T.R.Cooper, A.Cooper, S.L.Cox, D.Dixon, J.Gensmantel, N.Hamley, P.J.Harrison, R.Hartopp, P.Kack, H.Leeson, P.D.Luker, T.Mete, A.Millichip, I.Nicholls, D.J.Pimm, A.D.St-Gallay, S.A.Wallace, A.V.

(2011) Bioorg Med Chem Lett 21: 2468

  • DOI: https://doi.org/10.1016/j.bmcl.2011.02.061
  • Primary Citation of Related Structures:  
    2Y37, 4UX6

  • PubMed Abstract: 

    By careful analysis of experimental X-ray ligand crystallographic protein data across several inhibitor series we have discovered a novel, potent and selective series of iNOS inhibitors exemplified by compound 8.


  • Organizational Affiliation

    Department of Chemistry, AstraZeneca Charnwood, Bakewell Road, Loughborough LE11 5RH, United Kingdom. [email protected]


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
NITRIC OXIDE SYNTHASE, INDUCIBLE
A, B
433Mus musculusMutation(s): 0 
EC: 1.14.13.39
UniProt & NIH Common Fund Data Resources
Find proteins for P29477 (Mus musculus)
Explore P29477 
Go to UniProtKB:  P29477
IMPC:  MGI:97361
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29477
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 5 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
HEM
Query on HEM

Download Ideal Coordinates CCD File 
G [auth A],
L [auth B]
PROTOPORPHYRIN IX CONTAINING FE
C34 H32 Fe N4 O4
KABFMIBPWCXCRK-RGGAHWMASA-L
A54
Query on A54

Download Ideal Coordinates CCD File 
F [auth A],
K [auth B]
2-[(1R)-3-amino-1-phenyl-propoxy]-4-chloro-benzonitrile
C16 H15 Cl N2 O
GPCXUXJZOSOVLY-OAHLLOKOSA-N
H4B
Query on H4B

Download Ideal Coordinates CCD File 
H [auth A],
M [auth B]
5,6,7,8-TETRAHYDROBIOPTERIN
C9 H15 N5 O3
FNKQXYHWGSIFBK-RPDRRWSUSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
C [auth A],
D [auth A],
I [auth B]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
GOL
Query on GOL

Download Ideal Coordinates CCD File 
E [auth A],
J [auth B]
GLYCEROL
C3 H8 O3
PEDCQBHIVMGVHV-UHFFFAOYSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
A54 BindingDB:  2Y37 IC50: min: 4, max: 900 (nM) from 2 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.60 Å
  • R-Value Free: 0.242 
  • R-Value Work: 0.208 
  • R-Value Observed: 0.210 
  • Space Group: P 61 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 212.492α = 90
b = 212.492β = 90
c = 115.372γ = 120
Software Package:
Software NamePurpose
BUSTERrefinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Ligand Structure Quality Assessment 


Entry History 

Revision History  (Full details and data files)

  • Version 1.0: 2011-04-13
    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: 2018-01-17
    Changes: Data collection
  • Version 1.4: 2024-05-08
    Changes: Data collection, Database references, Derived calculations, Other