Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 3 (Q6DE94)
Analyse AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6DE94
- Type
- protein
- Length
- 618 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Nuclear cap-binding protein subunit 3
- UniProt
- Q6DE94
- Pockets
- 3 · best druggability 0.59
Structure
1 distinct chain · 24% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 3 | protein | 618 | 24% helix, 6% strand | Q6DE94 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.59 | 0.80 | 29 | empty |
| 2 | 334 | 0.54 | 0.75 | 32 | empty |
| 3 | 102 | 0.45 | 0.79 | 22 | 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 Q6DE94
- Elsewhere: UniProt Q6DE94 · AlphaFold DB Q6DE94
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