Research workbench
Cryo-EM structure of human apo CNGA1 channel in K+/CA2+
Analyse Cryo-EM structure of human apo CNGA1 channel in K+/CA2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LFT
- Type
- protein
- Length
- 1,800 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P29973
- Ligands
- CPL, CLR, K
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 450 | — | P29973 |
Ligands and binding sites
- CPL · 1-palmitoyl-2-linoleoyl-sn-glycero-3-phosphocholine · ligand · 24 copies · chains A, D, B, C
- CLR · Cholesterol · ligand · 8 copies · chains A, B, C, D
- K · Potassium ion · metal · 3 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7LFT · Cryo-EM structure of human Apo CNGA1 channel in K+/Ca2+ · 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 0.90
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
- Elsewhere: RCSB PDB 7LFT · PDBe 7LFT · UniProt P29973
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