Research workbench
Cryoem structure of the human KV4.2-KCHIP1 complex, transmembrane region
Analyse Cryoem structure of the human KV4.2-KCHIP1 complex, transmembrane region in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E7Z
- Type
- protein
- Length
- 992 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium voltage-gated channel subfamily D member 2
- UniProt
- Q9NZV8
- Pockets
- 17 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Potassium voltage-gated channel subfamily D member 2 | protein | 248 | 74% helix, 0% strand | Q9NZV8 |
Pockets
17 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 822 | 0.80 | 0.83 | 45 | empty |
| 2 | 520 | 0.66 | 0.77 | 53 | empty |
| 3 | 500 | 0.65 | 0.76 | 51 | empty |
| 4 | 518 | 0.65 | 0.76 | 57 | empty |
| 5 | 477 | 0.64 | 0.76 | 53 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1522 Ų buried · 4 hydrogen bonds · protein-protein
- A–D · 1521 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 1520 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 1507 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 24 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 7E7Z · CryoEM structure of the human Kv4.2-KChIP1 complex, transmembrane region · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NZV8 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily D member… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q9NZV8
- Elsewhere: RCSB PDB 7E7Z · PDBe 7E7Z · UniProt Q9NZV8
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