Research workbench
Allosteric peptides that bind to a caspase zymogen and mediate caspase tetramerization
Analyse Allosteric peptides that bind to a caspase zymogen and mediate caspase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EJF
- Type
- protein
- Length
- 1,019 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P55212
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 243 | — | P55212 |
| E, G, H | — | protein | 12 | — | — |
| F | — | protein | 11 | — | — |
Compared structures
- 4EJF · Allosteric peptides that bind to a caspase zymogen and mediate caspase tetramerization · the same entry in another collection · chain H against H, TM-score 1.00
- P55212 · AlphaFold monomer V2.0 prediction for caspase-6 (P55212) · a predicted model of the same protein · chain C against A, TM-score 0.95
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 P55212
- Elsewhere: RCSB PDB 4EJF · PDBe 4EJF · UniProt P55212
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