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Antibody-anti-idiotype complex: AP33 Fab (hepatitis C virus E2 antibody) - B2.1A scfv (anti-idiotype)

Analyse Antibody-anti-idiotype complex: AP33 Fab (hepatitis C virus E2 antibody)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SXI
Type
protein
Length
654 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab heavy chain; Fab light chain; Single chain fv - heavy chain; Single chain fv - light…
Pockets
7 · best druggability 0.65

Structure

x-ray diffraction · 4 distinct chains · 6% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HFab heavy chainprotein2126% helix, 54% strand—
LFab light chainprotein2156% helix, 53% strand—
ASingle chain fv - heavy chainprotein11910% helix, 50% strand—
BSingle chain fv - light chainprotein1083% helix, 46% strand—

Ligands and binding sites

  • GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16990.650.7564empty
2960.540.8421empty
31090.360.7323GOL
4660.300.7418empty
5710.290.7317empty

Interfaces

6 interfaces between chains.

  • H–L · 1908 Ų buried · 19 hydrogen bonds · protein-protein
  • A–B · 934 Ų buried · 8 hydrogen bonds · protein-protein
  • H–A · 398 Ų buried · 2 hydrogen bonds · protein-protein
  • L–A · 383 Ų buried · 6 hydrogen bonds · protein-protein
  • L–B · 252 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 6SXI · Antibody-anti-idiotype complex: AP33 Fab (hepatitis C virus E2 antibody) - B2.1A scFv… · the same entry in another collection · chain H against H, TM-score 1.00

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