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Designed tetrahedral nanoparticle T33-31 presenting BG505 sosip trimers

Analyse Designed tetrahedral nanoparticle T33-31 presenting BG505 sosip trimers in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7L85
Type
protein
Length
2,664 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
BG505 sosip-T33-31B; BG505 sosip-T33-31A
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 2 distinct chains · 32% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, C, E, G, I, K, M, O, Q, S, V, XBG505 sosip-T33-31Bprotein11830% helix, 27% strand—
A, D, F, H, J, L, N, P, R, T, W, YBG505 sosip-T33-31Aprotein10435% helix, 38% strand—

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11120.800.9718empty
21040.800.9718empty
31030.800.9718empty
41040.800.9719empty
59820.760.78102empty

Interfaces

48 interfaces between chains.

  • J–N · 1135 Ų buried · 13 hydrogen bonds · protein-protein
  • H–P · 1134 Ų buried · 14 hydrogen bonds · protein-protein
  • D–R · 1133 Ų buried · 14 hydrogen bonds · protein-protein
  • F–J · 1130 Ų buried · 14 hydrogen bonds · protein-protein
  • F–N · 1130 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 7L85 · Designed tetrahedral nanoparticle T33-31 presenting BG505 SOSIP trimers · the same entry in another collection · chain B against B, TM-score 1.00

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