Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1 (B3MS75)
Analyse AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B3MS75
- Type
- protein
- Length
- 800 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x26dEdD8528d07680013a2f005A1D1d358398e2E5
- Molecule
- Nuclear cap-binding protein subunit 1
- UniProt
- B3MS75
- Pockets
- 12 · best druggability 0.74
Structure
1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 1 | protein | 800 | 67% helix, 1% strand | B3MS75 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 487 | 0.74 | 0.82 | 47 | empty |
| 2 | 324 | 0.67 | 0.81 | 38 | empty |
| 3 | 277 | 0.63 | 0.81 | 25 | empty |
| 4 | 372 | 0.59 | 0.76 | 38 | empty |
| 5 | 112 | 0.41 | 0.76 | 16 | 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 B3MS75
- Elsewhere: UniProt B3MS75 · AlphaFold DB B3MS75
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