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FAB/EPITOPE complex structure of rabbit monoclonal antibody R53 targeting an epitope in HIV-1 GP120 C4 region

Analyse FAB/EPITOPE complex structure of rabbit monoclonal antibody R53 targeting an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ZTO
Type
protein
Length
895 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rabbit monoclonal antibody R53 Fab light chain; Rabbit monoclonal antibody R53 Fab heavy…
Pockets
9 · best druggability 0.67

Structure

x-ray diffraction · 4 distinct chains · 4% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
L, MRabbit monoclonal antibody R53 Fab light chainprotein2165% helix, 55% strand—
H, IRabbit monoclonal antibody R53 Fab heavy chainprotein2213% helix, 51% strand—
PEpitope of rabbit monoclonal antibody R53protein110% helix, 0% strand—
QEpitope of rabbit monoclonal antibody R53protein100% helix, 0% strand—

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13970.670.8049empty
25140.610.7454empty
34770.610.7549empty
4680.540.8619empty
52030.500.7623empty

Interfaces

9 interfaces between chains.

  • M–I · 2017 Ų buried · 22 hydrogen bonds · protein-protein
  • L–H · 2011 Ų buried · 21 hydrogen bonds · protein-protein
  • I–Q · 400 Ų buried · 3 hydrogen bonds · protein-protein
  • L–P · 397 Ų buried · 8 hydrogen bonds · protein-protein
  • H–I · 377 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

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