Research workbench
AlphaFold monomer V2.0 prediction for protein transport protein SEC23 (Q9C284)
Analyse AlphaFold monomer V2.0 prediction for protein transport protein SEC23 (Q9C284) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9C284
- Type
- protein
- Length
- 775 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- Protein transport protein SEC23
- UniProt
- Q9C284
- Pockets
- 15 · best druggability 0.66
Structure
1 distinct chain · 33% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein transport protein SEC23 | protein | 775 | 33% helix, 23% strand | Q9C284 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 418 | 0.66 | 0.79 | 51 | empty |
| 2 | 194 | 0.56 | 0.80 | 21 | empty |
| 3 | 196 | 0.53 | 0.78 | 24 | empty |
| 4 | 207 | 0.52 | 0.77 | 25 | empty |
| 5 | 161 | 0.52 | 0.79 | 25 | 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 Q9C284
- Elsewhere: UniProt Q9C284 · AlphaFold DB Q9C284
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