X-ray diffraction
2.7Å resolution

Crystal structure of VEGFR1 in complex with N-(4-Chlorophenyl)-2-((pyridin-4-ylmethyl)amino)benzamide

Source organism: Homo sapiens
Entry authors: Tresaugues L, Roos A, Arrowsmith CH, Berglund H, Bountra C, Collins R, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Johansson A, Johansson I, Karlberg T, Kotenyova T, Moche M, Nyman T, Persson C, Kragh-Nielsen T, Kotzch A, Sagemark J, Schueler H, Schutz P, Siponen MI, Svensson L, Thorsell AG, Van der Berg S, Weigelt J, Welin M, Wisniewska M, Nordlund P, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Vascular endothelial growth factor receptor 1 Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 41.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P17948 (Residues: 801-1158; Coverage: 27%)
Gene names: FLT, FLT1, FRT, VEGFR1
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I222
Unit cell:
a: 58.04Å b: 71.15Å c: 196.02Å
α: 90° β: 90° γ: 90°
R R work R free
0.197 0.194 0.26
Expression system: Escherichia coli