Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein VEIS_1053 (A1WGS2)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein VEIS_1053… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1WGS2
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Nucleotide-binding protein VEIS_1053
- UniProt
- A1WGS2
- Pockets
- 3 · best druggability 0.53
Structure
1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein VEIS_1053 | protein | 288 | 48% helix, 18% strand | A1WGS2 |
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 | 211 | 0.53 | 0.78 | 36 | empty |
| 2 | 199 | 0.48 | 0.75 | 27 | empty |
| 3 | 112 | 0.42 | 0.77 | 19 | 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 A1WGS2
- Elsewhere: UniProt A1WGS2 · AlphaFold DB A1WGS2
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