Research workbench
AlphaFold monomer V2.0 prediction for synaptotagmin-2 (P29101)
Analyse AlphaFold monomer V2.0 prediction for synaptotagmin-2 (P29101) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P29101
- Type
- protein
- Length
- 422 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3298b100681D3A2372Bba3b2f282750dD71629B9
- Molecule
- Synaptotagmin-2
- UniProt
- P29101
- Pockets
- 1 · best druggability 0.40
Structure
1 distinct chain · 19% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Synaptotagmin-2 | protein | 422 | 19% helix, 31% strand | P29101 |
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 | 74 | 0.40 | 0.78 | 14 | empty |
Compared structures
- 4ISR · Binding domain of Botulinum neurotoxin DC in complex with rat synaptotagmin II · an experimental structure of the same protein · chain A against D, TM-score 0.03
- 4ISR · Binding domain of botulinum neurotoxin dc in complex with rat synaptotagmin II · an experimental structure of the same protein · chain A against D, TM-score 0.03
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 P29101
- Elsewhere: UniProt P29101 · AlphaFold DB P29101
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