Research workbench
Human caspase-3 in complex with ac-ATS009-ke
Analyse Human caspase-3 in complex with ac-ATS009-ke in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CL0
- Type
- protein
- Length
- 255 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-3 subunit P17; Caspase-3 subunit P12; ACE-1MH-asp-PF5-phe-1U8
- EC
- 3.4.22.56
- UniProt
- P42574
- Ligands
- ACE
Structure
x-ray diffraction · 3 distinct chains · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-3 subunit P17 (EC 3.4.22.56) | protein | 146 | 26% helix, 29% strand | P42574 |
| B | Caspase-3 subunit P12 (EC 3.4.22.56) | protein | 104 | 30% helix, 16% strand | P42574 |
| C | ACE-1MH-asp-PF5-phe-1U8 | protein | 5 | 0% helix, 60% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 2219 Ų buried · 34 hydrogen bonds · protein-protein
- B–C · 457 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 216 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified, 1 covalent (nonstandard, 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 6CL0 · PDBe 6CL0 · UniProt P42574
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