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Crystal structure of the Fab fragment of an anti-DR5 antibody bound to DR5

Analyse Crystal structure of the Fab fragment of an anti-DR5 antibody bound to DR5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4OD2
Type
protein
Length
520 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fab fragment of drozitumab, light chain; Fab fragment of drozitumab, heavy chain; Tumor…
UniProt
O14763
Pockets
5 · best druggability 0.58

Structure

x-ray diffraction · 3 distinct chains · 4% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFab fragment of drozitumab, light chainprotein2096% helix, 51% strand—
BFab fragment of drozitumab, heavy chainprotein2145% helix, 52% strand—
STumor necrosis factor receptor superfamily member 10Bprotein970% helix, 29% strandO14763

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15070.580.7366empty
2520.380.8017empty
3590.370.7913empty
4950.340.7418empty
5720.320.7515empty

Interfaces

3 interfaces between chains.

  • A–B · 1642 Ų buried · 20 hydrogen bonds · protein-protein
  • A–S · 523 Ų buried · 10 hydrogen bonds · protein-protein
  • B–S · 508 Ų buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 disulfide (disulfide).

Compared structures

  • 4OD2 · Crystal structure of the Fab fragment of an anti-DR5 antibody bound to DR5 · the same entry in another collection · chain A against A, TM-score 1.00
  • O14763 · AlphaFold monomer V2.0 prediction for tumor necrosis factor receptor superfamily member… · a predicted model of the same protein · chain S against A, TM-score 0.92

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