Research workbench
Structure of the TRPA1 ion channel determined by electron cryo- microscopy
Analyse Structure of the TRPA1 ion channel determined by electron cryo- microscopy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J9P
- Type
- protein
- Length
- 2,240 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AEX9, O75762
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, A, B, C | — | protein | 560 | — | P0AEX9, O75762 |
Compared structures
- 3J9P · Structure of the TRPA1 ion channel determined by electron cryo-microscopy · the same entry in another collection · chain D against D, TM-score 1.00
- O75762 · AlphaFold monomer V2.0 prediction for transient receptor potential cation channel… · a predicted model of the same protein · chain D against A, TM-score 0.86
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 P0AEX9
- Every structure of UniProt O75762
- Elsewhere: RCSB PDB 3J9P · PDBe 3J9P · UniProt P0AEX9 · UniProt O75762
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