Research workbench
Human RIPK3 amyloid fibril revealed by solid-state NMR
Analyse Human RIPK3 amyloid fibril revealed by solid-state NMR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DAC
- Type
- protein
- Length
- 145 residues
- Chains
- 5
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor-interacting SERINE/THREONINE-protein kinase 3
- EC
- 2.7.11.1
- UniProt
- Q9Y572
- Pockets
- 2 · best druggability 0.44
Structure
solid-state nmr · 1 distinct chain · 0% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Receptor-interacting SERINE/THREONINE-protein kinase 3 (EC 2.7.11.1) | protein | 29 | 0% helix, 59% strand | Q9Y572 |
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 | 169 | 0.44 | 0.75 | 23 | empty |
| 2 | 75 | 0.33 | 0.74 | 20 | empty |
Interfaces
7 interfaces between chains.
- D–E · 1244 Ų buried · 31 hydrogen bonds · protein-protein
- B–C · 1211 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 1200 Ų buried · 32 hydrogen bonds · protein-protein
- A–B · 1178 Ų buried · 29 hydrogen bonds · protein-protein
- A–C · 20 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7DAC · Human RIPK3 amyloid fibril revealed by solid-state NMR · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y572 · AlphaFold monomer V2.0 prediction for receptor-interacting SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.26
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 7DAC · PDBe 7DAC · UniProt Q9Y572
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