Research workbench
Caspase-3:CAS26049945
Analyse Caspase-3:CAS26049945 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XYP
- Type
- protein
- Length
- 239 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-3 subunit P17; Caspase-3 subunit P12
- EC
- 3.4.22.56
- UniProt
- P42574
- Ligands
- XVE
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-3 subunit P17 (EC 3.4.22.56) | protein | 146 | 25% helix, 29% strand | P42574 |
| B | Caspase-3 subunit P12 (EC 3.4.22.56) | protein | 93 | 33% helix, 17% strand | P42574 |
Ligands and binding sites
- XVE · Phenylmethyl N-[(2S)-4-chloro-3-oxo-1-phenyl-butan-2-yl]carbamate · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 2167 Ų buried · 33 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 2XYP · PDBe 2XYP · UniProt P42574
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