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Crystal structure of antibody 93F3 unstable variant

Analyse Crystal structure of antibody 93F3 unstable variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4J1U
Type
protein
Length
1,262 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Antibody 93F3 light chain; Antibody 93F3 heavy chain
Pockets
17 · best druggability 0.74

Structure

x-ray diffraction · 6 distinct chains · 6% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAntibody 93F3 light chainprotein2106% helix, 52% strand—
BAntibody 93F3 heavy chainprotein2088% helix, 50% strand—
CAntibody 93F3 light chainprotein2134% helix, 50% strand—
DAntibody 93F3 heavy chainprotein2106% helix, 45% strand—
EAntibody 93F3 light chainprotein2146% helix, 52% strand—
FAntibody 93F3 heavy chainprotein2078% helix, 52% strand—

Pockets

17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16120.740.8160empty
26390.680.7762empty
35620.610.7457empty
43600.610.7733empty
52470.590.8035empty

Interfaces

9 interfaces between chains.

  • C–D · 1648 Ų buried · 16 hydrogen bonds · protein-protein
  • A–B · 1595 Ų buried · 15 hydrogen bonds · protein-protein
  • E–F · 1464 Ų buried · 12 hydrogen bonds · protein-protein
  • C–F · 637 Ų buried · 8 hydrogen bonds · protein-protein
  • A–D · 508 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 disulfide (disulfide).

Compared structures

  • 4J1U · Crystal structure of antibody 93F3 unstable variant · the same entry in another collection · chain A against A, TM-score 1.00

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