Research workbench
Structure of the pore domain of homomeric MLRRC8A volume-regulated anion channel at 3.66 a resolution
Analyse Structure of the pore domain of homomeric MLRRC8A volume-regulated anion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6G8Z
- Type
- protein
- Length
- 1,908 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q80WG5
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 318 | — | Q80WG5 |
Compared structures
- 6G8Z · Structure of the pore domain of homomeric mLRRC8A volume-regulated anion channel at 3.66… · the same entry in another collection · chain C against C, TM-score 1.00
- Q80WG5 · AlphaFold monomer V2.0 prediction for volume-regulated anion channel subunit LRRC8A… · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q80WG5
- Elsewhere: RCSB PDB 6G8Z · PDBe 6G8Z · UniProt Q80WG5
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