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Anti-P24 (HIV-1) Fab fragment CB41 complexed with an epitope-unrelated D-peptide

Analyse Anti-P24 (HIV-1) Fab fragment CB41 complexed with an epitope-unrelated D-peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1CFT
Type
protein
Length
432 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (IGG2A kappa antibody CB41 (light chain) ); Protein (IGG2A kappa antibody CB41…
Pockets
7 · best druggability 0.48

Structure

x-ray diffraction · 3 distinct chains · 5% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (IGG2A kappa antibody CB41 (light chain) )protein2146% helix, 50% strand—
BProtein (IGG2A kappa antibody CB41 (heavy chain) )protein2134% helix, 51% strand—
CProtein (antigen bound peptide)protein50% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11770.480.7630empty
21130.410.7624empty
3880.350.7517empty
4500.290.7612empty
5540.280.7413empty

Interfaces

3 interfaces between chains.

  • A–B · 1793 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 230 Ų buried · 2 hydrogen bonds · protein-protein
  • B–C · 221 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1CFT · Anti-P24 (HIV-1) Fab fragment CB41 complexed with an epitope-unrelated D-peptide · the same entry in another collection · chain B against B, TM-score 1.00

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