Research workbench
Cryo-EM structure of amyloid fibril formed by human RIPK3
Analyse Cryo-EM structure of amyloid fibril formed by human RIPK3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DA4
- Type
- protein
- Length
- 66 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-interacting SERINE/THREONINE-protein kinase 3
- EC
- 2.7.11.1
- UniProt
- Q9Y572
Structure
electron microscopy · 1 distinct chain · 0% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C | Receptor-interacting SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 22 | 0% helix, 5% strand | Q9Y572 |
Interfaces
3 interfaces between chains.
- B–A · 914 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 913 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 34 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7DA4 · Cryo-EM structure of amyloid fibril formed by human RIPK3 · the same entry in another collection · chain B against B, TM-score 1.00
- Q9Y572 · AlphaFold monomer V2.0 prediction for receptor-interacting SERINE/THREONINE-protein… · a predicted model of the same protein · chain B against A, TM-score 0.19
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 Q9Y572
- Elsewhere: RCSB PDB 7DA4 · PDBe 7DA4 · UniProt Q9Y572
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