Research workbench
Dual epitope targeting by anti-DR5 antibodies
Analyse Dual epitope targeting by anti-DR5 antibodies in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T3J
- Type
- protein
- Length
- 1,942 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IGG1-HDR5-01-heavy chain; IGG1-HDR5-01-light chain; IGG1-HDR5-05-heavy chain…
- UniProt
- O14763
- Pockets
- 20 · best druggability 0.59
Structure
x-ray diffraction · 8 distinct chains · 5% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | IGG1-HDR5-01-heavy chain | protein | 219 | 5% helix, 51% strand | — |
| B | IGG1-HDR5-01-light chain | protein | 212 | 7% helix, 50% strand | — |
| C | IGG1-HDR5-05-heavy chain | protein | 219 | 5% helix, 53% strand | — |
| D, I | IGG1-HDR5-05-light chain | protein | 210 | 7% helix, 50% strand | — |
| E | Tumor necrosis factor receptor superfamily member 10B | protein | 112 | 0% helix, 35% strand | O14763 |
| G | IGG1-HDR5-01-light chain | protein | 213 | 7% helix, 50% strand | — |
| H | IGG1-HDR5-05-heavy chain | protein | 218 | 6% helix, 53% strand | — |
| J | Tumor necrosis factor receptor superfamily member 10B | protein | 110 | 0% helix, 34% strand | O14763 |
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 322 | 0.59 | 0.77 | 42 | empty |
| 2 | 391 | 0.56 | 0.74 | 53 | empty |
| 3 | 358 | 0.55 | 0.74 | 49 | empty |
| 4 | 295 | 0.54 | 0.75 | 45 | empty |
| 5 | 67 | 0.54 | 0.87 | 25 | empty |
Interfaces
12 interfaces between chains.
- H–I · 2029 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1975 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1969 Ų buried · 18 hydrogen bonds · protein-protein
- F–G · 1928 Ų buried · 16 hydrogen bonds · protein-protein
- A–E · 587 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 29 disulfide, 2 modified (disulfide, phosphorylation).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O14763
- Elsewhere: RCSB PDB 6T3J · PDBe 6T3J · UniProt O14763
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