Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit D (C3L1A9)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit D (C3L1A9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3L1A9
- Type
- protein
- Length
- 216 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB44F19a0cb161828322eEEd13F55d4C3C34938d2
- Molecule
- V-type ATP synthase subunit D
- UniProt
- C3L1A9
- Pockets
- 1 · best druggability 0.46
Structure
1 distinct chain · 74% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase subunit D | protein | 216 | 74% helix, 9% strand | C3L1A9 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 148 | 0.46 | 0.76 | 21 | 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 C3L1A9
- Elsewhere: UniProt C3L1A9 · AlphaFold DB C3L1A9
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