MolNFT v1 · #154804 · protein
P22/P10 complex of caspase-11 mutant C254A
6KMU · Caspase-4: “P22/P10 complex of caspase-11 mutant C254A”. X-ray diffraction, 6 pockets (best druggability 0.84). MolNFT v1 #154804 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6KMU
- Type
- protein
- Length
- 1,002 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-4
- EC
- 3.4.22.64
- UniProt
- P70343
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 8 distinct chains · 30% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-4 (EC 3.4.22.64) | protein | 172 | 30% helix, 24% strand | P70343 |
| B | Caspase-4 (EC 3.4.22.64) | protein | 86 | 28% helix, 22% strand | P70343 |
| C | Caspase-4 (EC 3.4.22.64) | protein | 172 | 31% helix, 23% strand | P70343 |
| D | Caspase-4 (EC 3.4.22.64) | protein | 87 | 28% helix, 23% strand | P70343 |
| E | Caspase-4 (EC 3.4.22.64) | protein | 171 | 29% helix, 24% strand | P70343 |
| F | Caspase-4 (EC 3.4.22.64) | protein | 83 | 29% helix, 19% strand | P70343 |
| G | Caspase-4 (EC 3.4.22.64) | protein | 154 | 32% helix, 22% strand | P70343 |
| H | Caspase-4 (EC 3.4.22.64) | protein | 77 | 35% helix, 17% 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 | 1043 | 0.84 | 0.85 | 89 | empty |
| 2 | 82 | 0.40 | 0.78 | 15 | empty |
| 3 | 74 | 0.37 | 0.78 | 22 | empty |
| 4 | 94 | 0.34 | 0.73 | 20 | empty |
| 5 | 73 | 0.31 | 0.74 | 18 | empty |
Interfaces
17 interfaces between chains.
- A–B · 3123 Ų buried · 48 hydrogen bonds · protein-protein
- E–F · 3078 Ų buried · 54 hydrogen bonds · protein-protein
- C–D · 3056 Ų buried · 56 hydrogen bonds · protein-protein
- G–H · 2145 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 1518 Ų buried · 29 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 6KMU · PDBe 6KMU · UniProt P70343
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