Research workbench
Caspase-8 specific unnatural amino acid peptides
Analyse Caspase-8 specific unnatural amino acid peptides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PRZ
- Type
- protein
- Length
- 244 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Caspase-8; (ACE)LET(1U8) peptide
- EC
- 3.4.22.61
- UniProt
- Q14790
- Ligands
- ACE
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Caspase-8 (EC 3.4.22.61) | protein | 240 | 32% helix, 23% strand | Q14790 |
| B | (ACE)LET(1U8) peptide | 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
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.41 | 0.75 | 20 | empty |
| 2 | 50 | 0.27 | 0.74 | 13 | DTD |
Interfaces
1 interface between chains.
- A–B · 463 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 modified (covalent ligand, nonstandard).
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 Q14790
- Elsewhere: RCSB PDB 4PRZ · PDBe 4PRZ · UniProt Q14790
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