PDBe 2met

Solution NMR

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

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: P35968 (Residues: 759-795; Coverage: 3%)
Gene names: FLK1, KDR, VEGFR2

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