Research workbench
AlphaFold monomer V2.0 prediction for protein transport protein SEC23 (P0CR38)
Analyse AlphaFold monomer V2.0 prediction for protein transport protein SEC23 (P0CR38) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0CR38
- Type
- protein
- Length
- 763 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Protein transport protein SEC23
- UniProt
- P0CR38
- Pockets
- 10 · best druggability 0.72
Structure
1 distinct chain · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein transport protein SEC23 | protein | 763 | 33% helix, 24% strand | P0CR38 |
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.72 | 0.85 | 44 | empty |
| 2 | 452 | 0.68 | 0.79 | 56 | empty |
| 3 | 446 | 0.64 | 0.77 | 39 | empty |
| 4 | 230 | 0.64 | 0.83 | 23 | empty |
| 5 | 153 | 0.50 | 0.78 | 23 | 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 P0CR38
- Elsewhere: UniProt P0CR38 · AlphaFold DB P0CR38
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