4UWC

Fibroblast growth factor receptor 1 kinase in complex with JK-P3

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.179 

wwPDB Validation   3D Report Full Report


Ligand Structure Quality Assessment 


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


Literature

Validation of IMS-MS as a screening tool to identify type II kinase inhibitors of FGFR1 kinase.

Beeston, H.S., Klein, T., Norman, R.A., Tucker, J.A., Anderson, M., Ashcroft, A.E., Holdgate, G.A.

(2021) Rapid Commun Mass Spectrom : e9130-e9130

  • DOI: https://doi.org/10.1002/rcm.9130
  • Primary Citation of Related Structures:  
    4UWB, 4UWC

  • PubMed Abstract: 

    The protein kinase FGFR1 regulates cellular processes in human development. As over-activity of FGFR1 is implicated with cancer, effective inhibitors are in demand. Type I inhibitors, which bind to the active form of FGFR1, are less effective than type II inhibitors, which bind to the inactive form. Screening to distinguish between type I and type II inhibitors is required.

    • Organizational Affiliation: 

    Astbury Centre for Structural Molecular Biology & Faculty of Biological Sciences, University of Leeds, Leeds, LS2 9JT, UK.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
FIBROBLAST GROWTH FACTOR RECEPTOR 1
A, B
309Homo sapiensMutation(s): 2 
EC: 2.7.10.1
UniProt & NIH Common Fund Data Resources
Find proteins for P11362 (Homo sapiens)
Explore P11362 
Go to UniProtKB:  P11362
PHAROS:  P11362
GTEx:  ENSG00000077782 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP11362
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
4Y0
Query on 4Y0
Download Ideal Coordinates CCD File 
J [auth A],
V [auth B]		3,4-dimethoxy-N-(5-phenyl-1H-pyrazol-3-yl)benzamide
C18 H17 N3 O3
QAZJUVDICQNITG-UHFFFAOYSA-N
SO4
Query on SO4
Download Ideal Coordinates CCD File 
M [auth A]
N [auth A]
O [auth A]
P [auth A]
X [auth B]
M [auth A],
N [auth A],
O [auth A],
P [auth A],
X [auth B],
Y [auth B]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
PPI
Query on PPI
Download Ideal Coordinates CCD File 
K [auth A],
L [auth A],
W [auth B]		PROPANOIC ACID
C3 H6 O2
XBDQKXXYIPTUBI-UHFFFAOYSA-N
EDO
Query on EDO
Download Ideal Coordinates CCD File 
C [auth A]
D [auth A]
E [auth A]
F [auth A]
G [auth A]
C [auth A],
D [auth A],
E [auth A],
F [auth A],
G [auth A],
H [auth A],
I [auth A],
Q [auth B],
R [auth B],
S [auth B],
T [auth B],
U [auth B]
1,2-ETHANEDIOL
C2 H6 O2
LYCAIKOWRPUZTN-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.96 Å
  • R-Value Free: 0.206 
  • R-Value Work: 0.177 
  • R-Value Observed: 0.179 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 207.464α = 90
b = 58.422β = 107.38
c = 65.946γ = 90
Software Package:
Software NamePurpose
BUSTERrefinement
XDSdata reduction
SCALAdata scaling
PHASERphasing

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: 2015-09-02
    Type: Initial release
  • Version 1.1: 2017-03-29
    Changes: Other
  • Version 1.2: 2017-06-14
    Changes: Source and taxonomy
  • Version 1.3: 2021-06-16
    Changes: Database references, Derived calculations, Other, Refinement description