MolNFT v2 · #226485 · protein
Cryo-EM Structure of E-4031-bound hERG Channel
8ZYP · Potassium voltage-gated channel subfamily H member 2: “Cryo-EM Structure of E-4031-bound hERG Channel”. Electron microscopy at 3.19, 1 ligand (A1L2J), 16 pockets (best druggability 0.79). MolNFT v2 #226485 on GenesisL1: 3D…
- PDB
- 8ZYP
- Type
- protein
- Length
- 840 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.19
- Source
- Homo sapiens
- Molecule
- Potassium voltage-gated channel subfamily H member 2
- UniProt
- Q12809
- Ligands
- A1L2J
- Pockets
- 16 · best druggability 0.79
Structure
electron microscopy · resolution 3.19 · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Potassium voltage-gated channel subfamily H member 2 | protein | 210 | 74% helix, 0% strand | Q12809 |
Ligands and binding sites
- A1L2J · ~{N}-[4-[1-[2-(6-methylpyridin-2-yl)ethyl]piperidin-4-yl]carbonylphenyl]methanesulfonamide · ligand · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 706 | 0.79 | 0.84 | 63 | A1L2J |
| 2 | 158 | 0.47 | 0.76 | 17 | empty |
| 3 | 167 | 0.47 | 0.75 | 23 | empty |
| 4 | 129 | 0.46 | 0.78 | 19 | empty |
| 5 | 155 | 0.46 | 0.75 | 23 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1048 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 1047 Ų buried · 7 hydrogen bonds · protein-protein
- B–C · 1038 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 1028 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 29 Ų buried · 0 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 Q12809
- Elsewhere: RCSB PDB 8ZYP · PDBe 8ZYP · UniProt Q12809
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