Research workbench
AlphaFold monomer V2.0 prediction for V-type proton ATPase 16 kda proteolipid subunit (P63082)
Analyse AlphaFold monomer V2.0 prediction for V-type proton ATPase 16 kda proteolipid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P63082
- Type
- protein
- Length
- 155 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- V-type proton ATPase 16 kda proteolipid subunit
- UniProt
- P63082
Structure
1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type proton ATPase 16 kda proteolipid subunit | protein | 155 | 87% helix, 0% strand | P63082 |
Compared structures
- 9BRT · Intact V-ATPase State 1 and synaptophysin complex in mouse brain isolated synaptic… · an experimental structure of the same protein · chain A against n, TM-score 0.94
- 9BRZ · V0-only V-ATPase and synaptophysin complex in mouse brain isolated synaptic vesicles · an experimental structure of the same protein · chain A against m, TM-score 0.94
- 9BRY · V0-only V-ATPase in synaptophysin gene knock-out mouse brain isolated synaptic vesicles · an experimental structure of the same protein · chain A against o, TM-score 0.94
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 P63082
- Elsewhere: UniProt P63082 · AlphaFold DB P63082
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