Research workbench
AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit D 2 (Q6P335)
Analyse AlphaFold monomer V2.0 prediction for V-type proton ATPase subunit D 2 (Q6P335) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6P335
- Type
- protein
- Length
- 350 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd1A2963012bEcbC7A8f505464439Ab678C48936f
- Molecule
- V-type proton ATPase subunit D 2
- UniProt
- Q6P335
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type proton ATPase subunit D 2 | protein | 350 | 70% helix, 0% strand | Q6P335 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 448 | 0.64 | 0.77 | 46 | empty |
| 2 | 67 | 0.42 | 0.81 | 18 | empty |
| 3 | 72 | 0.33 | 0.75 | 12 | empty |
| 4 | 50 | 0.28 | 0.75 | 13 | 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 Q6P335
- Elsewhere: UniProt Q6P335 · AlphaFold DB Q6P335
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