Research workbench
AlphaFold monomer V2.0 prediction for nucleotide-binding protein SFUM_2066 (A0LJZ7)
Analyse AlphaFold monomer V2.0 prediction for nucleotide-binding protein SFUM_2066… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0LJZ7
- Type
- protein
- Length
- 286 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3A567c5ee0B5108637496d57c9632c932d9F229A
- Molecule
- Nucleotide-binding protein SFUM_2066
- UniProt
- A0LJZ7
- Pockets
- 4 · best druggability 0.50
Structure
1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleotide-binding protein SFUM_2066 | protein | 286 | 47% helix, 19% strand | A0LJZ7 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.50 | 0.78 | 28 | empty |
| 2 | 119 | 0.42 | 0.76 | 24 | empty |
| 3 | 68 | 0.40 | 0.80 | 16 | empty |
| 4 | 91 | 0.40 | 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 A0LJZ7
- Elsewhere: UniProt A0LJZ7 · AlphaFold DB A0LJZ7
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