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Crystal structure of vascular endothelial growth factor (VEGF8-109) with HH4, an ALPHA/BETA-peptide with irregular secondary structure

Analyse Crystal structure of vascular endothelial growth factor (VEGF8-109) with HH4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6D3O
Type
protein
Length
219 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Vascular endothelial growth factor a; HH4
UniProt
P15692
Pockets
2 · best druggability 0.45

Structure

x-ray diffraction · 4 distinct chains · 14% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVascular endothelial growth factor aprotein9611% helix, 63% strandP15692
BVascular endothelial growth factor aprotein9512% helix, 63% strandP15692
CHH4protein1527% helix, 0% strand—
DHH4protein1331% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11680.450.7543empty
2960.340.7326empty

Interfaces

5 interfaces between chains.

  • A–B · 1330 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 407 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 400 Ų buried · 6 hydrogen bonds · protein-protein
  • A–D · 122 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 107 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified, 7 disulfide (nonstandard, disulfide).

Compared structures

  • 6D3O · Crystal Structure of Vascular Endothelial Growth Factor (VEGF8-109) with HH4, an… · the same entry in another collection · chain A against A, TM-score 1.00

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