Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein CSAC_1160 (A4XIN0)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein CSAC_1160… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4XIN0
- Type
- protein
- Length
- 293 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x56071EB6171562445b8c56A46E20FbFb873E3C4d
- Molecule
- Nucleotide-binding protein CSAC_1160
- UniProt
- A4XIN0
- Pockets
- 4 · best druggability 0.50
Structure
1 distinct chain · 48% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein CSAC_1160 | protein | 293 | 48% helix, 17% strand | A4XIN0 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.50 | 0.77 | 24 | empty |
| 2 | 75 | 0.37 | 0.78 | 22 | empty |
| 3 | 73 | 0.35 | 0.76 | 17 | empty |
| 4 | 57 | 0.30 | 0.76 | 12 | 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 A4XIN0
- Elsewhere: UniProt A4XIN0 · AlphaFold DB A4XIN0
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