PDBe 2met

Solution NMR

NMR spatial structure of the trimeric mutant TM domain of VEGFR2 receptor.


Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Vascular endothelial growth factor receptor 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 37 amino acids
Theoretical weight: 4.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P35968 (Residues: 759-795; Coverage: 3%)
Gene names: FLK1, KDR, VEGFR2
Sequence domains: VEGFR-2 Transmembrane domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 32%
Refinement method: torsion angle dynamics
Chemical shifts: BMR19531  
Expression system: Escherichia coli