Research workbench
AlphaFold monomer V2.0 prediction for transmembrane protein 104 homolog (Q54S12)
Analyse AlphaFold monomer V2.0 prediction for transmembrane protein 104 homolog (Q54S12) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q54S12
- Type
- protein
- Length
- 499 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x43f3f7B2cb49a1b2aF0201708A2239ED4b2af5eb
- Molecule
- Transmembrane protein 104 homolog
- UniProt
- Q54S12
- Pockets
- 4 · best druggability 0.81
Structure
1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane protein 104 homolog | protein | 499 | 69% helix, 0% strand | Q54S12 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.81 | 0.96 | 34 | empty |
| 2 | 1110 | 0.74 | 0.77 | 70 | empty |
| 3 | 260 | 0.52 | 0.75 | 36 | empty |
| 4 | 86 | 0.44 | 0.80 | 16 | empty |
Modifications
Observed in the structure: 1 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 Q54S12
- Elsewhere: UniProt Q54S12 · AlphaFold DB Q54S12
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