Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein SAUSA300_0748 (Q2FIM8)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein SAUSA300_0748… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2FIM8
- Type
- protein
- Length
- 303 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf4ED13986579E8e227b3ED6c02276c648754EC27
- Molecule
- Nucleotide-binding protein SAUSA300_0748
- UniProt
- Q2FIM8
- Pockets
- 5 · best druggability 0.51
Structure
1 distinct chain · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein SAUSA300_0748 | protein | 303 | 47% helix, 18% strand | Q2FIM8 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.51 | 0.77 | 25 | empty |
| 2 | 105 | 0.47 | 0.80 | 18 | empty |
| 3 | 125 | 0.40 | 0.75 | 18 | empty |
| 4 | 117 | 0.38 | 0.75 | 17 | empty |
| 5 | 52 | 0.28 | 0.74 | 13 | 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 Q2FIM8
- Elsewhere: UniProt Q2FIM8 · AlphaFold DB Q2FIM8
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