Research workbench
AlphaFold monomer V2.0 prediction for high-affinity nickel-transport protein nixa (Q48262)
Analyse AlphaFold monomer V2.0 prediction for high-affinity nickel-transport protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q48262
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5d1DBE1CCF2C7b8d1a0c0376A6169d8E6d6f2603
- Molecule
- High-affinity nickel-transport protein nixa
- UniProt
- Q48262
- Pockets
- 6 · best druggability 0.63
Structure
1 distinct chain · 84% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High-affinity nickel-transport protein nixa | protein | 331 | 84% helix, 0% strand | Q48262 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 364 | 0.63 | 0.79 | 32 | empty |
| 2 | 249 | 0.60 | 0.80 | 33 | empty |
| 3 | 189 | 0.52 | 0.77 | 29 | empty |
| 4 | 68 | 0.39 | 0.79 | 14 | empty |
| 5 | 60 | 0.34 | 0.77 | 14 | 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 Q48262
- Elsewhere: UniProt Q48262 · AlphaFold DB Q48262
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