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The development of peptide-based tools for the analysis of angiogenesis

Analyse The development of peptide-based tools for the analysis of angiogenesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3S1K
Type
protein
Length
292 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Z-domain; Vascular endothelial growth factor a
UniProt
P15692
Pockets
2 · best druggability 0.43

Structure

x-ray diffraction · 3 distinct chains · 29% helix, 48% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BZ-domainprotein5281% helix, 0% strand—
VVascular endothelial growth factor aprotein9513% helix, 61% strandP15692
WVascular endothelial growth factor aprotein9316% helix, 60% strandP15692

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11650.430.7434empty
21170.380.7423empty

Interfaces

5 interfaces between chains.

  • V–W · 1343 Ų buried · 12 hydrogen bonds · protein-protein
  • B–V · 578 Ų buried · 6 hydrogen bonds · protein-protein
  • A–W · 554 Ų buried · 4 hydrogen bonds · protein-protein
  • A–V · 299 Ų buried · 4 hydrogen bonds · protein-protein
  • B–W · 285 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 3S1K · The Development of Peptide-based Tools for the Analysis of Angiogenesis · the same entry in another collection · chain A against A, TM-score 1.00

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