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Vegfr-2/VEGF-a complex structure

Analyse Vegfr-2/VEGF-a complex structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3V2A
Type
protein
Length
280 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.204
Source
Homo sapiens
Molecule
Vascular endothelial growth factor receptor 2; Vascular endothelial growth factor A
EC
2.7.10.1
UniProt
P35968, P15692
Pockets
3 · best druggability 0.34

Structure

x-ray diffraction · resolution 3.204 · 2 distinct chains · 5% helix, 58% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
RVascular endothelial growth factor receptor 2 (EC 2.7.10.1)protein1852% helix, 56% strandP35968
AVascular endothelial growth factor Aprotein9511% helix, 62% strandP15692

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1750.340.7519empty
2580.300.7516empty
3540.270.7313empty

Interfaces

1 interface between chains.

  • R–A · 698 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 3V2A · Vegfr-2/VEGF-a complex structure · the same entry in another collection · chain A against A, TM-score 1.00
  • P15692 · AlphaFold monomer V2.0 prediction for vascular endothelial growth factor a (P15692) · a predicted model of the same protein · chain A against A, TM-score 0.97
  • P35968 · AlphaFold monomer V2.0 prediction for vascular endothelial growth factor receptor 2… · a predicted model of the same protein · chain R against A, TM-score 0.94

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