Research workbench
AlphaFold monomer V2.0 prediction for signal peptidase complex catalytic subunit SEC11 (A4RGA1)
Analyse AlphaFold monomer V2.0 prediction for signal peptidase complex catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4RGA1
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xcd38ee57516af74F8e67f1085a39c3741e4C0cda
- Molecule
- Signal peptidase complex catalytic subunit SEC11
- UniProt
- A4RGA1
- Pockets
- 1 · best druggability 0.40
Structure
1 distinct chain · 35% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal peptidase complex catalytic subunit SEC11 | protein | 172 | 35% helix, 21% strand | A4RGA1 |
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 | 78 | 0.40 | 0.78 | 15 | 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 A4RGA1
- Elsewhere: UniProt A4RGA1 · AlphaFold DB A4RGA1
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