Research workbench
AlphaFold monomer V2.0 prediction for ring finger and transmembrane domain-containing protein 2 (Q5RAG4)
Analyse AlphaFold monomer V2.0 prediction for ring finger and transmembrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RAG4
- Type
- protein
- Length
- 444 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79F0532c301C16028699D7F801A4ff10AE318066
- Molecule
- Ring finger and transmembrane domain-containing protein 2
- UniProt
- Q5RAG4
- Pockets
- 4 · best druggability 0.62
Structure
1 distinct chain · 48% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ring finger and transmembrane domain-containing protein 2 | protein | 444 | 48% helix, 3% strand | Q5RAG4 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 370 | 0.62 | 0.78 | 41 | empty |
| 2 | 168 | 0.61 | 0.84 | 30 | empty |
| 3 | 89 | 0.32 | 0.72 | 17 | empty |
| 4 | 61 | 0.29 | 0.73 | 14 | empty |
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 Q5RAG4
- Elsewhere: UniProt Q5RAG4 · AlphaFold DB Q5RAG4
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