Research workbench
Structure of the human proton-activated chloride channel ASOR in desensitized conformation
Analyse Structure of the human proton-activated chloride channel ASOR in desensitized… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SQH
- Type
- protein
- Length
- 849 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.5
- Source
- Homo sapiens
- Molecule
- Proton-activated chloride channel
- UniProt
- Q9H813
- Ligands
- NAG
- Pockets
- 16 · best druggability 0.82
Structure
electron microscopy · resolution 2.5 · 1 distinct chain · 35% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Proton-activated chloride channel | protein | 283 | 35% helix, 36% strand | Q9H813 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 948 | 0.82 | 0.84 | 107 | empty |
| 2 | 54 | 0.68 | 0.97 | 28 | empty |
| 3 | 355 | 0.63 | 0.78 | 42 | empty |
| 4 | 344 | 0.62 | 0.78 | 42 | empty |
| 5 | 354 | 0.62 | 0.78 | 42 | empty |
Interfaces
3 interfaces between chains.
- B–C · 2176 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 2173 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 2166 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 glycan (N-glycosylation).
Compared structures
- Q9H813 · AlphaFold monomer V2.0 prediction for proton-activated chloride channel (Q9H813) · a predicted model of the same protein · chain A against A, TM-score 0.76
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 Q9H813
- Elsewhere: RCSB PDB 7SQH · PDBe 7SQH · UniProt Q9H813
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