Research workbench
AlphaFold monomer V2.0 prediction for NA(+)/H(+) antiporter nhaa (Q5NE91)
Analyse AlphaFold monomer V2.0 prediction for NA(+)/H(+) antiporter nhaa (Q5NE91) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5NE91
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x85eA5dCbE12BA159843085Adb62F5cd3041dEa01
- Molecule
- NA(+)/H(+) antiporter nhaa
- UniProt
- Q5NE91
- Pockets
- 5 · best druggability 0.60
Structure
1 distinct chain · 76% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NA(+)/H(+) antiporter nhaa | protein | 383 | 76% helix, 2% strand | Q5NE91 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.60 | 0.83 | 30 | empty |
| 2 | 159 | 0.52 | 0.79 | 22 | empty |
| 3 | 98 | 0.45 | 0.80 | 20 | empty |
| 4 | 107 | 0.44 | 0.77 | 16 | empty |
| 5 | 76 | 0.36 | 0.76 | 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 Q5NE91
- Elsewhere: UniProt Q5NE91 · AlphaFold DB Q5NE91
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