1VR2

HUMAN VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR 2 (KDR) KINASE DOMAIN

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Work: 0.215 
  • R-Value Observed: 0.215 

wwPDB Validation   3D Report Full Report


This is version 1.7 of the entry. See complete history. 


Literature

Crystal structure of the kinase domain of human vascular endothelial growth factor receptor 2: a key enzyme in angiogenesis.

McTigue, M.A., Wickersham, J.A., Pinko, C., Showalter, R.E., Parast, C.V., Tempczyk-Russell, A., Gehring, M.R., Mroczkowski, B., Kan, C.C., Villafranca, J.E., Appelt, K.

(1999) Structure 7: 319-330

  • DOI: https://doi.org/10.1016/s0969-2126(99)80042-2
  • Primary Citation of Related Structures:  
    1VR2

  • PubMed Abstract: 

    Angiogenesis is involved in tumor growth, macular degeneration, retinopathy and other diseases. Vascular endothelial growth factor (VEGF) stimulates angiogenesis by binding to specific receptors (VEGFRs) on the surface of vascular endothelial cells. VEGFRs are receptor tyrosine kinases that, like the platelet-derived growth factor receptors (PDGFRs), contain a large insert within the kinase domain.

    • Organizational Affiliation: 

    Agouron Pharmaceuticals, 3565 General Atomics Court, San Diego, CA 92121, USA. mctigue@agouron.com


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (VASCULAR ENDOTHELIAL GROWTH FACTOR RECEPTOR KINASE)316Homo sapiensMutation(s): 2 
EC: 2.7.1.112
UniProt & NIH Common Fund Data Resources
Find proteins for P35968 (Homo sapiens)
Explore P35968 
Go to UniProtKB:  P35968
PHAROS:  P35968
GTEx:  ENSG00000128052 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP35968
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
PTR
Query on PTR
A
L-PEPTIDE LINKINGC9 H12 N O6 PTYR
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Work: 0.215 
  • R-Value Observed: 0.215 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 95.41α = 90
b = 96.04β = 90
c = 38.22γ = 90
Software Package:
Software NamePurpose
AMoREphasing
X-PLORrefinement
DENZOdata reduction
SCALEPACKdata scaling

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-03-15
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-08-02
    Changes: Refinement description, Source and taxonomy
  • Version 1.4: 2021-11-03
    Changes: Database references
  • Version 1.5: 2022-12-21
    Changes: Database references
  • Version 1.6: 2023-09-20
    Changes: Data collection, Refinement description
  • Version 1.7: 2023-11-15
    Changes: Data collection