Research workbench
Caspase-3 mutant - D9A,D28A,S150E
Analyse Caspase-3 mutant - D9A,D28A,S150E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BG1
- Type
- protein
- Length
- 244 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-3; Ac-asp-glu-val-asp-cmk
- EC
- 3.4.22.56
- UniProt
- P42574
- Ligands
- ACE, NA, 0QE
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-3 (EC 3.4.22.56) | protein | 146 | 26% helix, 31% strand | P42574 |
| C | Caspase-3 (EC 3.4.22.56) | protein | 94 | 33% helix, 19% strand | P42574 |
| B | Ac-asp-glu-val-asp-cmk | protein | 4 | 0% helix, 50% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains C, B
- NA · Sodium ion · metal · chains A, C
- 0QE · Chloromethane · ion · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–C · 2215 Ų buried · 33 hydrogen bonds · protein-protein
- C–B · 409 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 221 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 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 6BG1 · PDBe 6BG1 · UniProt P42574
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