Research workbench
AlphaFold monomer V2.0 prediction for NA(+)/H(+) antiporter nhab (Q15S32)
Analyse AlphaFold monomer V2.0 prediction for NA(+)/H(+) antiporter nhab (Q15S32) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q15S32
- Type
- protein
- Length
- 526 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- NA(+)/H(+) antiporter nhab
- UniProt
- Q15S32
- Pockets
- 4 · best druggability 0.64
Structure
1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NA(+)/H(+) antiporter nhab | protein | 526 | 75% helix, 0% strand | Q15S32 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 210 | 0.64 | 0.83 | 35 | empty |
| 2 | 136 | 0.48 | 0.78 | 22 | empty |
| 3 | 67 | 0.41 | 0.79 | 14 | empty |
| 4 | 76 | 0.30 | 0.73 | 17 | 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 Q15S32
- Elsewhere: UniProt Q15S32 · AlphaFold DB Q15S32
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