Research workbench
Phosphorylation regulates assembly of the caspase-6 substrate-binding groove
Analyse Phosphorylation regulates assembly of the caspase-6 substrate-binding groove in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S8E
- Type
- protein
- Length
- 1,747 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-6
- EC
- 3.4.22.59
- UniProt
- P55212
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 8 distinct chains · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-6 (EC 3.4.22.59) | protein | 219 | 31% helix, 22% strand | P55212 |
| B | Caspase-6 (EC 3.4.22.59) | protein | 214 | 32% helix, 21% strand | P55212 |
| C | Caspase-6 (EC 3.4.22.59) | protein | 219 | 30% helix, 21% strand | P55212 |
| D | Caspase-6 (EC 3.4.22.59) | protein | 221 | 31% helix, 21% strand | P55212 |
| E | Caspase-6 (EC 3.4.22.59) | protein | 219 | 31% helix, 21% strand | P55212 |
| F | Caspase-6 (EC 3.4.22.59) | protein | 222 | 31% helix, 21% strand | P55212 |
| G | Caspase-6 (EC 3.4.22.59) | protein | 216 | 31% helix, 21% strand | P55212 |
| H | Caspase-6 (EC 3.4.22.59) | protein | 217 | 31% helix, 21% strand | P55212 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.72 | 0.86 | 53 | empty |
| 2 | 84 | 0.59 | 0.88 | 26 | empty |
| 3 | 148 | 0.58 | 0.83 | 30 | empty |
| 4 | 109 | 0.57 | 0.85 | 33 | empty |
| 5 | 231 | 0.56 | 0.78 | 33 | empty |
Interfaces
9 interfaces between chains.
- G–H · 1980 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 1955 Ų buried · 26 hydrogen bonds · protein-protein
- C–D · 1948 Ų buried · 23 hydrogen bonds · protein-protein
- E–F · 1942 Ų buried · 23 hydrogen bonds · protein-protein
- A–D · 799 Ų buried · 11 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 P55212
- Elsewhere: RCSB PDB 3S8E · PDBe 3S8E · UniProt P55212
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.