Research workbench
Crystal structure of caspase-6 inactivation mutation
Analyse Crystal structure of caspase-6 inactivation mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3V6L
- Type
- protein
- Length
- 480 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-6
- EC
- 3.4.22.59
- UniProt
- P55212
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-6 (EC 3.4.22.59) | protein | 239 | 29% helix, 26% strand | P55212 |
| B | Caspase-6 (EC 3.4.22.59) | protein | 241 | 30% helix, 26% strand | P55212 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.63 | 0.80 | 46 | empty |
| 2 | 79 | 0.52 | 0.85 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1525 Ų buried · 16 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 3V6L · PDBe 3V6L · UniProt P55212
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