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AlphaFold monomer V2.0 prediction for V-type proton ATPase 116 kda subunit A1 (A1A5G6)
Analyse AlphaFold monomer V2.0 prediction for V-type proton ATPase 116 kda subunit A1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1A5G6
- Type
- protein
- Length
- 837 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- V-type proton ATPase 116 kda subunit A1
- UniProt
- A1A5G6
- Pockets
- 13 · best druggability 0.69
Structure
1 distinct chain · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type proton ATPase 116 kda subunit A1 | protein | 837 | 61% helix, 8% strand | A1A5G6 |
Pockets
13 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.69 | 0.95 | 24 | empty |
| 2 | 324 | 0.64 | 0.80 | 37 | empty |
| 3 | 256 | 0.61 | 0.79 | 23 | empty |
| 4 | 283 | 0.51 | 0.74 | 24 | empty |
| 5 | 159 | 0.49 | 0.78 | 27 | 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 A1A5G6
- Elsewhere: UniProt A1A5G6 · AlphaFold DB A1A5G6
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