Research workbench
AlphaFold monomer V2.0 prediction for nuclear envelope integral membrane protein 1A (B9X187)
Analyse AlphaFold monomer V2.0 prediction for nuclear envelope integral membrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9X187
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9364A6372a080Fb5eCc644208c8e48C927a22807
- Molecule
- Nuclear envelope integral membrane protein 1A
- UniProt
- B9X187
- Pockets
- 2 · best druggability 0.50
Structure
1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear envelope integral membrane protein 1A | protein | 434 | 53% helix, 12% strand | B9X187 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.50 | 0.75 | 22 | empty |
| 2 | 150 | 0.49 | 0.78 | 29 | 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 B9X187
- Elsewhere: UniProt B9X187 · AlphaFold DB B9X187
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