Research workbench
Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated ion channel in complex with camp
Analyse Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U6P
- Type
- protein
- Length
- 2,092 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60741
- Ligands
- CMP
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 504 | — | O60741 |
| E, F, G, H | — | protein | 19 | — | — |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5U6P · Structure of the human HCN1 hyperpolarization-activated cyclic nucleotide-gated ion… · the same entry in another collection · chain H against H, TM-score 1.00
- O60741 · AlphaFold monomer V2.0 prediction for POTASSIUM/SODIUM hyperpolarization-activated cyclic… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 O60741
- Elsewhere: RCSB PDB 5U6P · PDBe 5U6P · UniProt O60741
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