Research workbench
AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit D (C3NEU1)
Analyse AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit D (C3NEU1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C3NEU1
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5881B09f2D8e743400698633641fc1cD2Ed2BE6F
- Molecule
- V-type ATP synthase subunit D
- UniProt
- C3NEU1
- Pockets
- 1 · best druggability 0.50
Structure
1 distinct chain · 77% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase subunit D | protein | 213 | 77% helix, 8% strand | C3NEU1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 184 | 0.50 | 0.76 | 20 | 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 C3NEU1
- Elsewhere: UniProt C3NEU1 · AlphaFold DB C3NEU1
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