Research workbench
AlphaFold monomer V2.0 prediction for UPF0210 protein BAD_1323 (A1A321)
Analyse AlphaFold monomer V2.0 prediction for UPF0210 protein BAD_1323 (A1A321) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1A321
- Type
- protein
- Length
- 454 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- UPF0210 protein BAD_1323
- UniProt
- A1A321
- Pockets
- 5 · best druggability 0.72
Structure
1 distinct chain · 48% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UPF0210 protein BAD_1323 | protein | 454 | 48% helix, 19% strand | A1A321 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.72 | 0.91 | 31 | empty |
| 2 | 124 | 0.44 | 0.76 | 14 | empty |
| 3 | 74 | 0.38 | 0.78 | 15 | empty |
| 4 | 68 | 0.33 | 0.76 | 12 | empty |
| 5 | 56 | 0.25 | 0.72 | 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 A1A321
- Elsewhere: UniProt A1A321 · AlphaFold DB A1A321
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