Research workbench
AlphaFold monomer V2.0 prediction for nuclear envelope integral membrane protein 1 (O14524)
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
- O14524
- Type
- protein
- Length
- 444 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- Nuclear envelope integral membrane protein 1
- UniProt
- O14524
- Pockets
- 4 · best druggability 0.52
Structure
1 distinct chain · 55% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear envelope integral membrane protein 1 | protein | 444 | 55% helix, 12% strand | O14524 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.52 | 0.75 | 30 | empty |
| 2 | 98 | 0.41 | 0.77 | 19 | empty |
| 3 | 92 | 0.38 | 0.76 | 13 | empty |
| 4 | 77 | 0.32 | 0.74 | 17 | 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 O14524
- Elsewhere: UniProt O14524 · AlphaFold DB O14524
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