Research workbench
AlphaFold monomer V2.0 prediction for V-set and transmembrane domain- containing protein 2-like protein (Q6PDS0)
Analyse AlphaFold monomer V2.0 prediction for V-set and transmembrane domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6PDS0
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- V-set and transmembrane domain-containing protein 2-like protein
- UniProt
- Q6PDS0
- Pockets
- 3 · best druggability 0.42
Structure
1 distinct chain · 17% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-set and transmembrane domain-containing protein 2-like protein | protein | 220 | 17% helix, 29% strand | Q6PDS0 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.42 | 0.73 | 28 | empty |
| 2 | 79 | 0.35 | 0.76 | 15 | empty |
| 3 | 71 | 0.27 | 0.72 | 13 | empty |
Modifications
Observed in the structure: 1 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 Q6PDS0
- Elsewhere: UniProt Q6PDS0 · AlphaFold DB Q6PDS0
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