Research workbench
P20/P12 of caspase-11 mutant C254A
Analyse P20/P12 of caspase-11 mutant C254A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KN1
- Type
- protein
- Length
- 494 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Mus musculus
- Molecule
- Caspase-4
- EC
- 3.4.22.64
- UniProt
- P70343
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · resolution 1.9 · 4 distinct chains · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-4 (EC 3.4.22.64) | protein | 164 | 32% helix, 23% strand | P70343 |
| B | Caspase-4 (EC 3.4.22.64) | protein | 87 | 28% helix, 18% strand | P70343 |
| C | Caspase-4 (EC 3.4.22.64) | protein | 155 | 30% helix, 23% strand | P70343 |
| D | Caspase-4 (EC 3.4.22.64) | protein | 88 | 27% helix, 19% strand | P70343 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 274 | 0.75 | 0.88 | 24 | empty |
| 2 | 89 | 0.35 | 0.75 | 16 | empty |
| 3 | 77 | 0.35 | 0.76 | 23 | empty |
| 4 | 70 | 0.34 | 0.76 | 16 | empty |
| 5 | 70 | 0.31 | 0.74 | 17 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2694 Ų buried · 46 hydrogen bonds · protein-protein
- C–D · 2402 Ų buried · 41 hydrogen bonds · protein-protein
- B–D · 1534 Ų buried · 29 hydrogen bonds · protein-protein
- A–D · 493 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 410 Ų buried · 8 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 P70343
- Elsewhere: RCSB PDB 6KN1 · PDBe 6KN1 · UniProt P70343
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