Research workbench
AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2-a (B4M205)
Analyse AlphaFold monomer V2.0 prediction for nuclear cap-binding protein subunit 2-a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4M205
- Type
- protein
- Length
- 154 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8DD805493e22E8987a3BbCDFeD5cc3a28Cd35b3f
- Molecule
- Nuclear cap-binding protein subunit 2-a
- UniProt
- B4M205
- Pockets
- 1 · best druggability 0.52
Structure
1 distinct chain · 30% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear cap-binding protein subunit 2-a | protein | 154 | 30% helix, 21% strand | B4M205 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.52 | 0.80 | 18 | 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 B4M205
- Elsewhere: UniProt B4M205 · AlphaFold DB B4M205
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