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Structure of anti-lasv Fab 25.10C with fnqi mutation

Analyse Structure of anti-lasv Fab 25.10C with fnqi mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7S8G
Type
protein
Length
838 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
25.10C-fnqi Fab heavy chain; 25.10C-fnqi Fab light chain
Pockets
7 · best druggability 0.74

Structure

x-ray diffraction · 3 distinct chains · 7% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
H25.10C-fnqi Fab heavy chainprotein2125% helix, 54% strand—
L, l25.10C-fnqi Fab light chainprotein2097% helix, 50% strand—
h25.10C-fnqi Fab heavy chainprotein2088% helix, 51% strand—

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16210.740.8166empty
23090.700.8437empty
32520.630.8135empty
43020.580.7744empty
53500.570.7646empty

Interfaces

6 interfaces between chains.

  • H–L · 1088 Ų buried · 15 hydrogen bonds · protein-protein
  • h–l · 962 Ų buried · 13 hydrogen bonds · protein-protein
  • H–l · 944 Ų buried · 4 hydrogen bonds · protein-protein
  • L–h · 883 Ų buried · 4 hydrogen bonds · protein-protein
  • H–h · 702 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 7S8G · Structure of anti-LASV Fab 25.10C with FNQI mutation · the same entry in another collection · chain H against H, TM-score 1.00

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