Research workbench
AlphaFold monomer V2.0 prediction for nuclear rim protein 1 (B3LGY4)
Analyse AlphaFold monomer V2.0 prediction for nuclear rim protein 1 (B3LGY4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B3LGY4
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x025f3b1a898b05AD2731bE6Ab72687b5920c4A3F
- Molecule
- Nuclear rim protein 1
- UniProt
- B3LGY4
- Pockets
- 5 · best druggability 0.46
Structure
1 distinct chain · 52% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear rim protein 1 | protein | 484 | 52% helix, 7% strand | B3LGY4 |
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 228 | 0.46 | 0.73 | 30 | empty |
| 2 | 116 | 0.43 | 0.76 | 18 | empty |
| 3 | 58 | 0.31 | 0.76 | 11 | empty |
| 4 | 54 | 0.26 | 0.73 | 13 | empty |
| 5 | 60 | 0.26 | 0.72 | 11 | 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 B3LGY4
- Elsewhere: UniProt B3LGY4 · AlphaFold DB B3LGY4
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