Research workbench
AlphaFold monomer V2.0 prediction for transmembrane protein 245 (E1BD52)
Analyse AlphaFold monomer V2.0 prediction for transmembrane protein 245 (E1BD52) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- E1BD52
- Type
- protein
- Length
- 868 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Transmembrane protein 245
- UniProt
- E1BD52
- Pockets
- 8 · best druggability 0.67
Structure
1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transmembrane protein 245 | protein | 868 | 74% helix, 0% strand | E1BD52 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.67 | 0.76 | 58 | empty |
| 2 | 291 | 0.59 | 0.77 | 35 | empty |
| 3 | 159 | 0.49 | 0.77 | 19 | empty |
| 4 | 52 | 0.40 | 0.82 | 16 | empty |
| 5 | 133 | 0.40 | 0.73 | 18 | 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 E1BD52
- Elsewhere: UniProt E1BD52 · AlphaFold DB E1BD52
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