Research workbench
AlphaFold monomer V2.0 prediction for nucleoid-associated protein VC0395_A1624/VC395_2154 (A5F6M1)
Analyse AlphaFold monomer V2.0 prediction for nucleoid-associated protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5F6M1
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x41f108fA06D265DE995730b2D626Bd9440871B04
- Molecule
- Nucleoid-associated protein VC0395_A1624/VC395_2154
- UniProt
- A5F6M1
- Pockets
- 2 · best druggability 0.56
Structure
1 distinct chain · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoid-associated protein VC0395_A1624/VC395_2154 | protein | 333 | 40% helix, 28% strand | A5F6M1 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.56 | 0.77 | 29 | empty |
| 2 | 78 | 0.38 | 0.77 | 15 | 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 A5F6M1
- Elsewhere: UniProt A5F6M1 · AlphaFold DB A5F6M1
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