Research workbench
Structural basis for dimerization of the death effector domains of caspase-8
Analyse Structural basis for dimerization of the death effector domains of caspase-8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H33
- Type
- protein
- Length
- 362 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-8
- EC
- 3.4.22.61
- UniProt
- Q14790
- Pockets
- 7 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Caspase-8 (EC 3.4.22.61) | protein | 181 | 66% helix, 2% strand | Q14790 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 220 | 0.52 | 0.77 | 39 | empty |
| 2 | 102 | 0.44 | 0.78 | 23 | empty |
| 3 | 117 | 0.41 | 0.76 | 15 | empty |
| 4 | 65 | 0.32 | 0.75 | 15 | empty |
| 5 | 76 | 0.31 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 3031 Ų buried · 15 hydrogen bonds · protein-protein
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 Q14790
- Elsewhere: RCSB PDB 5H33 · PDBe 5H33 · UniProt Q14790
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