Research workbench
N-terminal domain, voltage-gated potassium channel KV1.2 residues 33-119
Analyse N-terminal domain, voltage-gated potassium channel KV1.2 residues 33-119 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QDW
- Type
- protein
- Length
- 696 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KV1.2 voltage-gated potassium channel
- UniProt
- P63142
- Pockets
- 6 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | KV1.2 voltage-gated potassium channel | protein | 87 | 33% helix, 21% strand | P63142 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1084 | 0.83 | 0.84 | 77 | empty |
| 2 | 882 | 0.82 | 0.84 | 79 | empty |
| 3 | 540 | 0.69 | 0.79 | 48 | empty |
| 4 | 109 | 0.36 | 0.74 | 20 | empty |
| 5 | 107 | 0.35 | 0.73 | 24 | empty |
Interfaces
10 interfaces between chains.
- E–H · 739 Ų buried · 25 hydrogen bonds · protein-protein
- A–C · 739 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 721 Ų buried · 20 hydrogen bonds · protein-protein
- B–D · 714 Ų buried · 21 hydrogen bonds · protein-protein
- E–G · 713 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 1QDW · N-terminal domain, voltage-gated potassium channel KV1.2 residues 33-119 · the same entry in another collection · chain E against E, TM-score 1.00
- P63142 · AlphaFold monomer V2.0 prediction for potassium voltage-gated channel subfamily a member… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P63142
- Elsewhere: RCSB PDB 1QDW · PDBe 1QDW · UniProt P63142
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