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Anti-CD28XCD3 codv Fab bound to CD28

Analyse Anti-CD28XCD3 codv Fab bound to CD28 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6O8D
Type
protein
Length
796 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
T-cell-specific surface glycoprotein CD28; Anti-CD28XCD3 codv Fab light chain…
UniProt
P10747
Ligands
NAG
Pockets
11 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 5% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CT-cell-specific surface glycoprotein CD28protein1153% helix, 38% strandP10747
LAnti-CD28XCD3 codv Fab light chainprotein3384% helix, 39% strand—
HAnti-CD28XCD3 codv Fab heavy chainprotein3436% helix, 45% strand—

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11740.790.9424empty
26260.750.8162empty
35050.630.7635empty
42510.590.7935empty
5760.570.8726empty

Interfaces

3 interfaces between chains.

  • L–H · 2860 Ų buried · 27 hydrogen bonds · protein-protein
  • C–H · 292 Ų buried · 4 hydrogen bonds · protein-protein
  • C–L · 196 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 9 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6O8D · Anti-CD28xCD3 CODV Fab bound to CD28 · the same entry in another collection · chain C against C, TM-score 1.00
  • P10747 · AlphaFold monomer V2.0 prediction for T-cell-specific surface glycoprotein CD28 (P10747) · a predicted model of the same protein · chain C against A, TM-score 0.89

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