MolNFT v1 · #285687 · protein
AlphaFold monomer V2.0 prediction for proton-activated chloride channel (Q9H813)
Q9H813: “AlphaFold monomer V2.0 prediction for proton-activated chloride channel (Q9H813)”. 3 pockets (best druggability 0.44). MolNFT v1 #285687 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q9H813
- Type
- protein
- Length
- 350 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x196C286b0017BF4535E094dDd7e0ACAC05852e70
- Molecule
- Proton-activated chloride channel
- UniProt
- Q9H813
- Pockets
- 3 · best druggability 0.44
Structure
1 distinct chain · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proton-activated chloride channel | protein | 350 | 35% helix, 30% strand | Q9H813 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.44 | 0.73 | 19 | empty |
| 2 | 89 | 0.43 | 0.79 | 18 | empty |
| 3 | 61 | 0.34 | 0.76 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 7SQG · Structure of the human proton-activated chloride channel asor in resting conformation · an experimental structure of the same protein · chain A against A, TM-score 0.65
- 7JNA · Cryo-EM structure of human proton-activated chloride channel pac at pH 8 · an experimental structure of the same protein · chain A against A, TM-score 0.64
- 7SQH · Structure of the human proton-activated chloride channel ASOR in desensitized conformation · an experimental structure of the same protein · chain A against A, TM-score 0.62
- 7JNC · Cryo-EM structure of human proton-activated chloride channel pac at pH 4 · an experimental structure of the same protein · chain A against A, TM-score 0.61
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: UniProt Q9H813 · AlphaFold DB Q9H813
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