Research workbench
AlphaFold monomer V2.0 prediction for signal peptidase complex catalytic subunit SEC11C (Q9BY50)
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
- Q9BY50
- Type
- protein
- Length
- 192 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6C482d01F32F98784942cF1f954fA8aEba65C2c1
- Molecule
- Signal peptidase complex catalytic subunit SEC11C
- UniProt
- Q9BY50
- Pockets
- 1 · best druggability 0.38
Structure
1 distinct chain · 36% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal peptidase complex catalytic subunit SEC11C | protein | 192 | 36% helix, 20% strand | Q9BY50 |
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 | 71 | 0.38 | 0.78 | 14 | empty |
Compared structures
- 7P2Q · Human signal peptidase complex paralog C (spc-C) · an experimental structure of the same protein · chain A against A, TM-score 0.67
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 Q9BY50
- Elsewhere: UniProt Q9BY50 · AlphaFold DB Q9BY50
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