Research workbench
AlphaFold monomer V2.0 prediction for sodium-dependent phosphate transport protein 2C (Q8N130)
Analyse AlphaFold monomer V2.0 prediction for sodium-dependent phosphate transport… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8N130
- Type
- protein
- Length
- 599 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x848B622B139c7fB5ce26ccA19998c6cB362c7C6b
- Molecule
- Sodium-dependent phosphate transport protein 2C
- UniProt
- Q8N130
- Pockets
- 8 · best druggability 0.68
Structure
1 distinct chain · 64% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sodium-dependent phosphate transport protein 2C | protein | 599 | 64% helix, 2% strand | Q8N130 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 857 | 0.68 | 0.74 | 64 | empty |
| 2 | 332 | 0.65 | 0.80 | 35 | empty |
| 3 | 103 | 0.51 | 0.82 | 21 | empty |
| 4 | 134 | 0.45 | 0.76 | 26 | empty |
| 5 | 119 | 0.44 | 0.77 | 19 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q8N130
- Elsewhere: UniProt Q8N130 · AlphaFold DB Q8N130
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