Research workbench
AlphaFold monomer V2.0 prediction for nuclear envelope integral membrane protein 1 (A7MBC7)
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
- A7MBC7
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD98b781Af594e457Ce9D77D41fAbB92144b0Fc1d
- Molecule
- Nuclear envelope integral membrane protein 1
- UniProt
- A7MBC7
- Pockets
- 3 · best druggability 0.50
Structure
1 distinct chain · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear envelope integral membrane protein 1 | protein | 445 | 54% helix, 12% strand | A7MBC7 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 212 | 0.50 | 0.75 | 29 | empty |
| 2 | 220 | 0.50 | 0.75 | 27 | empty |
| 3 | 59 | 0.42 | 0.81 | 12 | 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 A7MBC7
- Elsewhere: UniProt A7MBC7 · AlphaFold DB A7MBC7
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