Research workbench
Structure of caspase-1 in complex with gasdermin D
Analyse Structure of caspase-1 in complex with gasdermin D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VIE
- Type
- protein
- Length
- 1,032 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29466, Q9D8T2
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 182 | — | P29466 |
| B | — | protein | 88 | — | P29466 |
| C | — | protein | 389 | — | Q9D8T2 |
| D | — | protein | 373 | — | Q9D8T2 |
Compared structures
- 6VIE · Structure of caspase-1 in complex with gasdermin D · the same entry in another collection · chain D against D, TM-score 1.00
- P29466 · AlphaFold monomer V2.0 prediction for caspase-1 (P29466) · a predicted model of the same protein · chain B against A, TM-score 0.96
- Q9D8T2 · AlphaFold monomer V2.0 prediction for gasdermin-D (Q9D8T2) · a predicted model of the same protein · chain C against A, TM-score 0.80
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 P29466
- Every structure of UniProt Q9D8T2
- Elsewhere: RCSB PDB 6VIE · PDBe 6VIE · UniProt P29466 · UniProt Q9D8T2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.