Research workbench
Mouse receptor-interacting protein kinase 3 (RIP3) amyloid structure by solid-state NMR
Analyse Mouse receptor-interacting protein kinase 3 (RIP3) amyloid structure by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JPD
- Type
- protein
- Length
- 105 residues
- Chains
- 5
- Method
- solid-state nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Mus musculus
- Molecule
- Receptor-interacting serine/threonine-protein kinase 3
- EC
- 2.7.11.1
- UniProt
- Q9QZL0
- Pockets
- 1 · best druggability 0.28
Structure
solid-state nmr · resolution NOT · 1 distinct chain · 0% helix, 29% 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 | 21 | 0% helix, 29% strand | Q9QZL0 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.28 | 0.72 | 16 | empty |
Interfaces
4 interfaces between chains.
- A–B · 890 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 890 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 890 Ų buried · 24 hydrogen bonds · protein-protein
- D–E · 890 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 6JPD · Mouse receptor-interacting protein kinase 3 (RIP3) amyloid structure by solid-state NMR · the same entry in another collection · chain A against A, TM-score 1.00
- Q9QZL0 · AlphaFold monomer V2.0 prediction for receptor-interacting SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.19
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 Q9QZL0
- Elsewhere: RCSB PDB 6JPD · PDBe 6JPD · UniProt Q9QZL0
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