Research workbench
AlphaFold monomer V2.0 prediction for signal peptidase complex catalytic subunit SEC11 (Q7RY44)
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
- Q7RY44
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD8D28A040FBDd4fb271E64aaE6BF15F7e59D0A8E
- Molecule
- Signal peptidase complex catalytic subunit SEC11
- UniProt
- Q7RY44
- Pockets
- 1 · best druggability 0.42
Structure
1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal peptidase complex catalytic subunit SEC11 | protein | 172 | 37% helix, 21% strand | Q7RY44 |
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 | 95 | 0.42 | 0.77 | 20 | 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 Q7RY44
- Elsewhere: UniProt Q7RY44 · AlphaFold DB Q7RY44
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