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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
- 5H31
- Type
- protein
- Length
- 728 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-8
- EC
- 3.4.22.61
- UniProt
- Q14790
- Pockets
- 12 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Caspase-8 (EC 3.4.22.61) | protein | 182 | 64% helix, 2% strand | Q14790 |
Pockets
12 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 818 | 0.69 | 0.76 | 71 | empty |
| 2 | 367 | 0.57 | 0.75 | 32 | empty |
| 3 | 155 | 0.47 | 0.77 | 19 | empty |
| 4 | 93 | 0.39 | 0.76 | 15 | empty |
| 5 | 98 | 0.36 | 0.74 | 18 | empty |
Interfaces
4 interfaces between chains.
- C–D · 3031 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 3007 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 494 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 178 Ų buried · 1 hydrogen bond · 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 5H31 · PDBe 5H31 · UniProt Q14790
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