MolNFT v1 · #188980 · protein
Crystal structure of caspase-3 with peptide inhibitor acitvkd-cho
7USO · Caspase-3 subunit P17: “Crystal structure of caspase-3 with peptide inhibitor acitvkd-cho”. X-ray diffraction, 1 ligand (ACE), 1 pocket (best druggability 0.67). MolNFT v1 #188980 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7USO
- Type
- protein
- Length
- 474 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-3 subunit P17; Caspase-3 subunit P12; Peptide inhibitor acitvkd-cho
- EC
- 3.4.22.56
- UniProt
- P42574
- Ligands
- ACE
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 4 distinct chains · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-3 subunit P17 (EC 3.4.22.56) | protein | 139 | 27% helix, 32% strand | P42574 |
| B, D | Caspase-3 subunit P12 | protein | 92 | 34% helix, 21% strand | P42574 |
| C | Caspase-3 subunit P17 (EC 3.4.22.56) | protein | 141 | 28% helix, 32% strand | P42574 |
| F, G | Peptide inhibitor acitvkd-cho | protein | 5 | 0% helix, 60% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains B, F, D, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 330 | 0.67 | 0.81 | 38 | empty |
Interfaces
10 interfaces between chains.
- C–D · 2208 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 2170 Ų buried · 31 hydrogen bonds · protein-protein
- B–D · 1463 Ų buried · 19 hydrogen bonds · protein-protein
- B–F · 500 Ų buried · 14 hydrogen bonds · protein-protein
- D–G · 494 Ų buried · 13 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 7USO · PDBe 7USO · UniProt P42574
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