Research workbench
Structure of the Caspase-8/cFLIP death effector domain assembly
Analyse Structure of the Caspase-8/cFLIP death effector domain assembly in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8YNL
- Type
- protein
- Length
- 1,583 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.55
- Source
- Homo sapiens
- Molecule
- Caspase-8 subunit p10; CASP8 and FADD-like apoptosis regulator subunit p43
- UniProt
- Q14790, O15519
- Pockets
- 20 · best druggability 0.74
Structure
electron microscopy · resolution 3.55 · 5 distinct chains · 64% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Caspase-8 subunit p10 | protein | 182 | 64% helix, 0% strand | Q14790 |
| H | CASP8 and FADD-like apoptosis regulator subunit p43 | protein | 172 | 65% helix, 1% strand | O15519 |
| I | CASP8 and FADD-like apoptosis regulator subunit p43 | protein | 170 | 66% helix, 0% strand | O15519 |
| J | CASP8 and FADD-like apoptosis regulator subunit p43 | protein | 170 | 65% helix, 0% strand | O15519 |
| K, G, F | CASP8 and FADD-like apoptosis regulator subunit p43 | protein | 175 | 62% helix, 1% strand | O15519 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 925 | 0.74 | 0.78 | 76 | empty |
| 2 | 362 | 0.68 | 0.82 | 68 | empty |
| 3 | 533 | 0.68 | 0.78 | 53 | empty |
| 4 | 567 | 0.68 | 0.77 | 51 | empty |
| 5 | 80 | 0.65 | 0.92 | 15 | empty |
Interfaces
19 interfaces between chains.
- A–H · 905 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 749 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 697 Ų buried · 9 hydrogen bonds · protein-protein
- G–F · 670 Ų buried · 5 hydrogen bonds · protein-protein
- J–K · 658 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- O15519 · AlphaFold monomer V2.0 prediction for CASP8 and fadd-like apoptosis regulator (O15519) · a predicted model of the same protein · chain I against A, TM-score 0.97
- Q14790 · AlphaFold monomer V2.0 prediction for caspase-8 (Q14790) · a predicted model of the same protein · chain C against A, TM-score 0.97
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 Q14790
- Every structure of UniProt O15519
- Elsewhere: RCSB PDB 8YNL · PDBe 8YNL · UniProt Q14790 · UniProt O15519
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