Research workbench
The structure of full-length kv beta 2.1 determined by cryogenic electron microscopy
Analyse The structure of full-length kv beta 2.1 determined by cryogenic electron… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CI1
- Type
- protein
- Length
- 2,608 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Voltage-gated potassium channel subunit beta-2
- EC
- 1.1.1.-
- UniProt
- P62483
- Pockets
- 7 · best druggability 0.45
Structure
electron microscopy · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Voltage-gated potassium channel subunit beta-2 (EC 1.1.1.-) | protein | 326 | 0% helix, 0% strand | P62483 |
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 176 | 0.45 | 0.73 | 41 | empty |
| 2 | 125 | 0.40 | 0.73 | 34 | empty |
| 3 | 120 | 0.39 | 0.73 | 32 | empty |
| 4 | 119 | 0.38 | 0.72 | 35 | empty |
| 5 | 103 | 0.37 | 0.72 | 31 | empty |
Interfaces
12 interfaces between chains.
- A–B · 65 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 62 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 59 Ų buried · 0 hydrogen bonds · protein-protein
- C–E · 59 Ų buried · 0 hydrogen bonds · protein-protein
- B–H · 55 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6CI1 · The Structure of Full-Length Kv Beta 2.1 Determined by Cryogenic Electron Microscopy · the same entry in another collection · chain H against H, TM-score 1.00
- P62483 · AlphaFold monomer V2.0 prediction for voltage-gated potassium channel subunit beta-2… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P62483
- Elsewhere: RCSB PDB 6CI1 · PDBe 6CI1 · UniProt P62483
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