Research workbench
AlphaFold monomer V2.0 prediction for nucleoid-associated protein yejk (B1X884)
Analyse AlphaFold monomer V2.0 prediction for nucleoid-associated protein yejk (B1X884) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1X884
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Nucleoid-associated protein yejk
- UniProt
- B1X884
- Pockets
- 4 · best druggability 0.45
Structure
1 distinct chain · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoid-associated protein yejk | protein | 335 | 40% helix, 28% strand | B1X884 |
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 | 207 | 0.45 | 0.74 | 26 | empty |
| 2 | 68 | 0.38 | 0.78 | 16 | empty |
| 3 | 76 | 0.33 | 0.75 | 15 | empty |
| 4 | 63 | 0.31 | 0.75 | 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 B1X884
- Elsewhere: UniProt B1X884 · AlphaFold DB B1X884
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