Research workbench
Crystal structure of death effector domain of CASPASE8 in homo sapiens
Analyse Crystal structure of death effector domain of CASPASE8 in homo sapiens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZBW
- Type
- protein
- Length
- 366 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
- 5 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Caspase-8 (EC 3.4.22.61) | protein | 183 | 63% helix, 2% strand | Q14790 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 539 | 0.63 | 0.75 | 46 | empty |
| 2 | 122 | 0.39 | 0.74 | 22 | empty |
| 3 | 70 | 0.32 | 0.75 | 15 | empty |
| 4 | 88 | 0.32 | 0.73 | 16 | empty |
| 5 | 55 | 0.28 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 504 Ų buried · 12 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 4ZBW · PDBe 4ZBW · UniProt Q14790
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