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Cryo-EM structure of ENAC

Analyse Cryo-EM structure of ENAC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BQN
Type
protein
Length
1,815 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SCNN1A; SCNN1B; Egfp-SCNN1G chimera; 7B1 Fab; 10D4 Fab
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 7 distinct chains · 22% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASCNN1Aprotein43926% helix, 20% strand—
BSCNN1Bprotein47930% helix, 23% strand—
CEgfp-SCNN1G chimeraprotein44330% helix, 22% strand—
D7B1 Fabprotein1060% helix, 42% strand—
E7B1 Fabprotein1215% helix, 41% strand—
F10D4 Fabprotein1150% helix, 36% strand—
G10D4 Fabprotein1123% helix, 21% strand—

Pockets

20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111380.860.8799empty
24280.860.9358empty
35210.850.9163empty
44360.810.8946empty
510180.810.82114empty

Interfaces

9 interfaces between chains.

  • A–B · 3239 Ų buried · 39 hydrogen bonds · protein-protein
  • B–C · 3055 Ų buried · 24 hydrogen bonds · protein-protein
  • A–C · 2565 Ų buried · 27 hydrogen bonds · protein-protein
  • B–F · 442 Ų buried · 1 hydrogen bond · protein-protein
  • A–E · 440 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 25 disulfide (disulfide).

Compared structures

  • 6BQN · Cryo-EM structure of ENaC · the same entry in another collection · chain A against A, TM-score 1.00

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