Research workbench
AlphaFold monomer V2.0 prediction for protein transport protein SEC23A (A2VDL8)
Analyse AlphaFold monomer V2.0 prediction for protein transport protein SEC23A (A2VDL8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2VDL8
- Type
- protein
- Length
- 768 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDFc598304c98686161aF975D39EA996Fe921C44
- Molecule
- Protein transport protein SEC23A
- UniProt
- A2VDL8
- Pockets
- 15 · best druggability 0.70
Structure
1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein transport protein SEC23A | protein | 768 | 33% helix, 24% strand | A2VDL8 |
Pockets
15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 468 | 0.70 | 0.80 | 59 | empty |
| 2 | 214 | 0.64 | 0.83 | 26 | empty |
| 3 | 158 | 0.57 | 0.82 | 24 | empty |
| 4 | 200 | 0.54 | 0.78 | 19 | empty |
| 5 | 237 | 0.52 | 0.76 | 26 | 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 A2VDL8
- Elsewhere: UniProt A2VDL8 · AlphaFold DB A2VDL8
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