MolNFT v2 · #221958 · protein
HCN1 nanodisc
8UC8 · Potassium/sodium hyperpolarization-activated cyclic…: “HCN1 nanodisc”. Electron microscopy at 3.0, 1 ligand (PCW), 20 pockets (best druggability 0.77). MolNFT v2 #221958 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8UC8
- Type
- protein
- Length
- 1,936 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.0
- Source
- Homo sapiens
- Molecule
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1
- UniProt
- O60741
- Ligands
- PCW
- Pockets
- 20 · best druggability 0.77
Structure
electron microscopy · resolution 3.0 · 1 distinct chain · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, C, A, B | Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 | protein | 484 | 62% helix, 9% strand | O60741 |
Ligands and binding sites
- PCW · 1,2-dioleoyl-sn-glycero-3-phosphocholine · ligand · 16 copies · chains D, C, A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1188 | 0.77 | 0.79 | 123 | empty |
| 2 | 1125 | 0.76 | 0.78 | 107 | PCW |
| 3 | 930 | 0.75 | 0.78 | 93 | PCW |
| 4 | 1178 | 0.75 | 0.77 | 122 | PCW |
| 5 | 1182 | 0.75 | 0.77 | 114 | PCW |
Interfaces
6 interfaces between chains.
- A–B · 3008 Ų buried · 29 hydrogen bonds · protein-protein
- D–A · 3005 Ų buried · 30 hydrogen bonds · protein-protein
- D–C · 3005 Ų buried · 30 hydrogen bonds · protein-protein
- C–B · 3005 Ų buried · 30 hydrogen bonds · protein-protein
- D–B · 451 Ų buried · 6 hydrogen bonds · protein-protein
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 8UC8 · PDBe 8UC8 · UniProt O60741
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