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MolNFT v1 · #25375 · protein

Complex between VEGF and a receptor blocking peptide

1VPP · Protein (vascular endothelial growth factor): “Complex between VEGF and a receptor blocking peptide”. X-ray diffraction, 3 pockets (best druggability 0.49). MolNFT v1 #25375 on GenesisL1: 3D structure, binding sites and pockets in…

PDB
1VPP
Type
protein
Length
224 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (vascular endothelial growth factor); Protein (peptide V108)
UniProt
P15692
Pockets
3 · best druggability 0.49

Structure

x-ray diffraction · 4 distinct chains · 9% helix, 59% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
VProtein (vascular endothelial growth factor)protein9613% helix, 60% strandP15692
WProtein (vascular endothelial growth factor)protein909% helix, 67% strandP15692
XProtein (peptide V108)protein200% helix, 40% strand—
YProtein (peptide V108)protein180% helix, 39% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11300.490.7927empty
2780.350.7623empty
3580.260.7218empty

Interfaces

5 interfaces between chains.

  • V–W · 1449 Ų buried · 9 hydrogen bonds · protein-protein
  • V–X · 664 Ų buried · 20 hydrogen bonds · protein-protein
  • W–Y · 541 Ų buried · 13 hydrogen bonds · protein-protein
  • V–Y · 57 Ų buried · 0 hydrogen bonds · protein-protein
  • W–X · 51 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

  • 1VPP · Complex between VEGF and a receptor blocking peptide · the same entry in another collection · chain V against V, 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 V against A, TM-score 0.93

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