Research workbench
AlphaFold monomer V2.0 prediction for signal peptide peptidase-like 3 (Q4V3B8)
Analyse AlphaFold monomer V2.0 prediction for signal peptide peptidase-like 3 (Q4V3B8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q4V3B8
- Type
- protein
- Length
- 540 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x22DeA0165442d1707E30933D5954EFC9Ee6e5849
- Molecule
- Signal peptide peptidase-like 3
- UniProt
- Q4V3B8
- Pockets
- 5 · best druggability 0.84
Structure
1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Signal peptide peptidase-like 3 | protein | 540 | 52% helix, 13% strand | Q4V3B8 |
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1054 | 0.84 | 0.85 | 87 | empty |
| 2 | 778 | 0.71 | 0.77 | 62 | empty |
| 3 | 73 | 0.52 | 0.85 | 23 | empty |
| 4 | 169 | 0.50 | 0.77 | 24 | empty |
| 5 | 65 | 0.30 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q4V3B8
- Elsewhere: UniProt Q4V3B8 · AlphaFold DB Q4V3B8
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