Research workbench
AlphaFold monomer V2.0 prediction for secretory carrier-associated membrane protein 1 (Q8H5X5)
Analyse AlphaFold monomer V2.0 prediction for secretory carrier-associated membrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8H5X5
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Secretory carrier-associated membrane protein 1
- UniProt
- Q8H5X5
- Pockets
- 2 · best druggability 0.36
Structure
1 distinct chain · 64% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Secretory carrier-associated membrane protein 1 | protein | 306 | 64% helix, 1% strand | Q8H5X5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.36 | 0.76 | 13 | empty |
| 2 | 52 | 0.28 | 0.74 | 11 | 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 Q8H5X5
- Elsewhere: UniProt Q8H5X5 · AlphaFold DB Q8H5X5
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