Research workbench
AlphaFold monomer V2.0 prediction for phosphonates import ATP-binding protein phnc 1 (Q16BC5)
Analyse AlphaFold monomer V2.0 prediction for phosphonates import ATP-binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q16BC5
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbff27Dc0a932A6E0d9Fe883AAbD1BF27bB95A69F
- Molecule
- Phosphonates import ATP-binding protein phnc 1
- UniProt
- Q16BC5
- Pockets
- 3 · best druggability 0.45
Structure
1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphonates import ATP-binding protein phnc 1 | protein | 263 | 41% helix, 23% strand | Q16BC5 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.45 | 0.75 | 21 | empty |
| 2 | 140 | 0.43 | 0.76 | 17 | empty |
| 3 | 50 | 0.28 | 0.75 | 10 | 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 Q16BC5
- Elsewhere: UniProt Q16BC5 · AlphaFold DB Q16BC5
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