Research workbench
Full-length human ENAC ecd
Analyse Full-length human ENAC ecd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WTH
- Type
- protein
- Length
- 1,594 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amiloride-sensitive sodium channel subunit alpha; Amiloride-sensitive sodium channel…
- UniProt
- P37088, P51168, P51170
- Ligands
- NAG, NA
- Pockets
- 20 · best druggability 0.90
Structure
electron microscopy · 7 distinct chains · 18% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amiloride-sensitive sodium channel subunit alpha | protein | 381 | 22% helix, 28% strand | P37088 |
| B | Amiloride-sensitive sodium channel subunit beta | protein | 413 | 26% helix, 29% strand | P51168 |
| C | Amiloride-sensitive sodium channel subunit gamma | protein | 389 | 25% helix, 28% strand | P51170 |
| D | 7B1 Fab | protein | 105 | 0% helix, 36% strand | — |
| E | 7B1 Fab | protein | 118 | 0% helix, 43% strand | — |
| F | 10D4 Fab | protein | 115 | 0% helix, 43% strand | — |
| G | 10D4 Fab | protein | 73 | 0% helix, 21% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains B, C, A
- NA · Sodium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1102 | 0.90 | 0.92 | 122 | empty |
| 2 | 552 | 0.87 | 0.93 | 67 | empty |
| 3 | 1039 | 0.86 | 0.87 | 105 | empty |
| 4 | 455 | 0.82 | 0.89 | 50 | empty |
| 5 | 863 | 0.80 | 0.83 | 104 | empty |
Interfaces
9 interfaces between chains.
- B–C · 2682 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 2616 Ų buried · 31 hydrogen bonds · protein-protein
- A–C · 2488 Ų buried · 24 hydrogen bonds · protein-protein
- B–F · 525 Ų buried · 6 hydrogen bonds · protein-protein
- A–E · 466 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 25 disulfide, 7 glycan (disulfide, N-glycosylation).
Compared structures
- 6WTH · Full-length human ENaC ECD · the same entry in another collection · chain G against G, TM-score 1.00
- P51168 · AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit beta… · a predicted model of the same protein · chain B against A, TM-score 0.99
- P37088 · AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit alpha… · a predicted model of the same protein · chain A against A, TM-score 0.98
- P51170 · AlphaFold monomer V2.0 prediction for amiloride-sensitive sodium channel subunit gamma… · a predicted model of the same protein · chain C against A, TM-score 0.97
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 P37088
- Every structure of UniProt P51168
- Every structure of UniProt P51170
- Elsewhere: RCSB PDB 6WTH · PDBe 6WTH · UniProt P37088 · UniProt P51168 · UniProt P51170
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.