Research workbench
Cryo-EM structure of human rod CNGA1/B1 channel in apo state
Analyse Cryo-EM structure of human rod CNGA1/B1 channel in apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RH9
- Type
- protein
- Length
- 1,792 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29973, Q14028
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 450 | — | P29973 |
| B | — | protein | 432 | — | Q14028 |
| A | — | protein | 456 | — | P29973 |
| D | — | protein | 454 | — | P29973 |
Compared structures
- 7RH9 · Cryo-EM structure of human rod CNGA1/B1 channel in apo state · the same entry in another collection · chain D against D, TM-score 1.00
- P29973 · AlphaFold monomer V2.0 prediction for cgmp-gated cation channel alpha-1 (P29973) · a predicted model of the same protein · chain A against A, TM-score 0.92
- Q14028 · AlphaFold monomer V2.0 prediction for cyclic nucleotide-gated cation channel beta-1… · a predicted model of the same protein · chain B against A, TM-score 0.92
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 P29973
- Every structure of UniProt Q14028
- Elsewhere: RCSB PDB 7RH9 · PDBe 7RH9 · UniProt P29973 · UniProt Q14028
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