Research workbench
Allosteric modulation of caspase-3 through mutagenesis
Analyse Allosteric modulation of caspase-3 through mutagenesis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EHF
- Type
- protein
- Length
- 246 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-3; ACE-asp-glu-val-asp-chloromethylketone inhibitor
- EC
- 3.4.22.56
- UniProt
- P42574
- Ligands
- ACE, 0QE
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-3 (EC 3.4.22.56) | protein | 242 | 29% helix, 26% strand | P42574 |
| B | ACE-asp-glu-val-asp-chloromethylketone inhibitor | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.42 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 471 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 P42574
- Elsewhere: RCSB PDB 4EHF · PDBe 4EHF · UniProt P42574
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