Research workbench
Cryo-EM structure of human KCNQ4
Analyse Cryo-EM structure of human KCNQ4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BYL
- Type
- protein
- Length
- 2,000 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Green fluorescent PROTEIN,POTASSIUM voltage-gated channel subfamily kqt member 4…
- UniProt
- P56696, P0DP25
- Ligands
- PT5, K
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 2 distinct chains · 73% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Green fluorescent PROTEIN,POTASSIUM voltage-gated channel subfamily kqt member 4 | protein | 354 | 79% helix, 0% strand | P56696 |
| B, D, F, H | Calmodulin-3 | protein | 146 | 58% helix, 7% strand | P0DP25 |
Ligands and binding sites
- PT5 · (1S)-2-{[(R)-hydroxy{[(1r,2r,3s,4r,5r,6s)-2,3,6-trihydroxy-4,5-bis(phosphonooxy) cyclohexyl]oxy}phosphoryl]oxy}-1-[(octadecanoyloxy) methyl]ethyl (8E,11E)-icosa-5,8,11,14-tetraenoate · ligand · 4 copies · chains A, C, E, G
- K · Potassium ion · metal · 4 copies · chains A, C, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 738 | 0.86 | 0.89 | 100 | K |
| 2 | 995 | 0.80 | 0.81 | 73 | PT5 |
| 3 | 885 | 0.79 | 0.81 | 96 | empty |
| 4 | 113 | 0.79 | 0.97 | 21 | empty |
| 5 | 246 | 0.75 | 0.88 | 37 | empty |
Interfaces
10 interfaces between chains.
- C–D · 2499 Ų buried · 28 hydrogen bonds · protein-protein
- E–F · 2496 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 2490 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 2479 Ų buried · 28 hydrogen bonds · protein-protein
- E–G · 2350 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 P56696
- Every structure of UniProt P0DP25
- Elsewhere: RCSB PDB 7BYL · PDBe 7BYL · UniProt P56696 · UniProt P0DP25
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