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Vaccine-elicited mouse fp-targeting neutralizing antibody VFP16.02 with F60P mutation on light chain in complex with HIV fusion peptide (residue 512-519)

Analyse Vaccine-elicited mouse fp-targeting neutralizing antibody VFP16.02 with F60P… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6WX2
Type
protein
Length
872 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
VFP16.02 antibody heavy chain; VFP16.02 antibody light chain; Fusion peptide
Pockets
11 · best druggability 0.66

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, HVFP16.02 antibody heavy chainprotein2107% helix, 54% strand—
B, LVFP16.02 antibody light chainprotein2186% helix, 51% strand—
C, FFusion peptideprotein80% helix, 0% strand—

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13540.660.8149empty
24720.610.7650empty
32460.600.8047empty
42560.600.8046empty
51640.510.7924empty

Interfaces

9 interfaces between chains.

  • H–L · 1856 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 1842 Ų buried · 14 hydrogen bonds · protein-protein
  • A–H · 1009 Ų buried · 8 hydrogen bonds · protein-protein
  • H–F · 371 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 365 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 6WX2 · Vaccine-elicited mouse FP-targeting neutralizing antibody vFP16.02 with F60P mutation on… · the same entry in another collection · chain A against A, TM-score 1.00

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