MolNFT v1 · #421594 · protein
AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit gamma (P51170)
P51170: “AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit gamma (P51170)”. 7 pockets (best druggability 0.62). MolNFT v1 #421594 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P51170
- Type
- protein
- Length
- 649 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x40B9C9d5F084D34d026E9d5Dd10501AcdF6d6152
- Molecule
- Amiloride-sensitive sodium channel subunit gamma
- UniProt
- P51170
- Pockets
- 7 · best druggability 0.62
Structure
1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amiloride-sensitive sodium channel subunit gamma | protein | 649 | 36% helix, 21% strand | P51170 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 379 | 0.62 | 0.77 | 38 | empty |
| 2 | 251 | 0.56 | 0.77 | 30 | empty |
| 3 | 190 | 0.45 | 0.74 | 30 | empty |
| 4 | 170 | 0.42 | 0.73 | 25 | empty |
| 5 | 56 | 0.37 | 0.80 | 16 | empty |
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 9BTU · Human SCNN1B-SCNN1G ENaC dimers · an experimental structure of the same protein · chain A against C, TM-score 0.60
- 6WTH · Full-length human ENAC ecd · an experimental structure of the same protein · chain A against C, TM-score 0.58
- 6WTH · Full-length human ENaC ECD · an experimental structure of the same protein · chain A against C, TM-score 0.58
- 9BLR · Human SCNN1D-SCNN1B-SCNN1G ENaC trimer · an experimental structure of the same protein · chain A against C, TM-score 0.57
- 9BTG · Human SCNN1B-SCNN1B-SCNN1G ENaC trimer · an experimental structure of the same protein · chain A against C, TM-score 0.57
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 P51170
- Elsewhere: UniProt P51170 · AlphaFold DB P51170
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