Research workbench
Cryo-EM reconstruction of caspase-1 card
Analyse Cryo-EM reconstruction of caspase-1 card in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FNA
- Type
- protein
- Length
- 680 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-1
- EC
- 3.4.22.36
- UniProt
- P29466
- Pockets
- 15 · best druggability 0.87
Structure
electron microscopy · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Caspase-1 (EC 3.4.22.36) | protein | 85 | 68% helix, 0% strand | P29466 |
Pockets
15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 876 | 0.87 | 0.89 | 103 | empty |
| 2 | 1006 | 0.86 | 0.86 | 97 | empty |
| 3 | 788 | 0.85 | 0.88 | 87 | empty |
| 4 | 1144 | 0.83 | 0.84 | 101 | empty |
| 5 | 621 | 0.79 | 0.84 | 70 | empty |
Interfaces
16 interfaces between chains.
- A–E · 606 Ų buried · 8 hydrogen bonds · protein-protein
- B–F · 605 Ų buried · 8 hydrogen bonds · protein-protein
- D–H · 604 Ų buried · 8 hydrogen bonds · protein-protein
- C–G · 598 Ų buried · 8 hydrogen bonds · protein-protein
- B–E · 344 Ų buried · 5 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 P29466
- Elsewhere: RCSB PDB 5FNA · PDBe 5FNA · UniProt P29466
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