Research workbench
AlphaFold monomer V2.0 prediction for burp domain protein RD22 (Q08298)
Analyse AlphaFold monomer V2.0 prediction for burp domain protein RD22 (Q08298) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q08298
- Type
- protein
- Length
- 392 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x772cDF339c71f2E91A7B5C3137d74bF9134420C6
- Molecule
- Burp domain protein RD22
- UniProt
- Q08298
- Pockets
- 6 · best druggability 0.57
Structure
1 distinct chain · 17% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Burp domain protein RD22 | protein | 392 | 17% helix, 29% strand | Q08298 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.57 | 0.85 | 16 | empty |
| 2 | 128 | 0.53 | 0.81 | 27 | empty |
| 3 | 143 | 0.48 | 0.78 | 19 | empty |
| 4 | 93 | 0.36 | 0.75 | 16 | empty |
| 5 | 58 | 0.33 | 0.77 | 16 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 Q08298
- Elsewhere: UniProt Q08298 · AlphaFold DB Q08298
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