Research workbench
Structure of the human homo-hexameric LRRC8D channel at 4.36 ångströms
Analyse Structure of the human homo-hexameric LRRC8D channel at 4.36 ångströms in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M04
- Type
- protein
- Length
- 4,282 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Volume-regulated anion channel subunit LRRC8D
- UniProt
- Q7L1W4
- Pockets
- 20 · best druggability 0.87
Structure
electron microscopy · 2 distinct chains · 37% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E | Volume-regulated anion channel subunit LRRC8D | protein | 714 | 38% helix, 8% strand | Q7L1W4 |
| C, F | Volume-regulated anion channel subunit LRRC8D | protein | 713 | 37% helix, 7% strand | Q7L1W4 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 352 | 0.87 | 0.95 | 58 | empty |
| 2 | 346 | 0.86 | 0.94 | 60 | empty |
| 3 | 430 | 0.85 | 0.92 | 72 | empty |
| 4 | 388 | 0.84 | 0.92 | 61 | empty |
| 5 | 814 | 0.82 | 0.84 | 93 | empty |
Interfaces
6 interfaces between chains.
- D–E · 3441 Ų buried · 32 hydrogen bonds · protein-protein
- A–B · 3438 Ų buried · 32 hydrogen bonds · protein-protein
- B–C · 2901 Ų buried · 32 hydrogen bonds · protein-protein
- E–F · 2898 Ų buried · 32 hydrogen bonds · protein-protein
- C–D · 1337 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6M04 · Structure of the human homo-hexameric LRRC8D channel at 4.36 Angstroms · the same entry in another collection · chain C against C, TM-score 1.00
- Q7L1W4 · AlphaFold monomer V2.0 prediction for volume-regulated anion channel subunit LRRC8D… · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q7L1W4
- Elsewhere: RCSB PDB 6M04 · PDBe 6M04 · UniProt Q7L1W4
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