Research workbench
K2P2.1 (trek-1), 10 mm K+
Analyse K2P2.1 (trek-1), 10 mm K+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W7D
- Type
- protein
- Length
- 525 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel subfamily K member 2
- UniProt
- P97438
- Ligands
- D12, LNK, R16, CD, K
- Pockets
- 14 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 77% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel subfamily K member 2 | protein | 251 | 78% helix, 0% strand | P97438 |
| B | Potassium channel subfamily K member 2 | protein | 274 | 75% helix, 0% strand | P97438 |
Ligands and binding sites
- D12 · Dodecane · ligand · 3 copies · chains A, B
- LNK · Pentane · ligand · 2 copies · chains B
- R16 · Hexadecane · ligand · chains A, B
- CD · Cadmium ion · metal · 3 copies · chains B
- K · Potassium ion · metal · 2 copies · chains A, B
- OCT · N-octane · additive · 5 copies · chains A, B
- 1PE · Pentaethylene glycol · additive
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.67 | 0.77 | 38 | empty |
| 2 | 212 | 0.66 | 0.84 | 41 | empty |
| 3 | 369 | 0.65 | 0.79 | 46 | empty |
| 4 | 150 | 0.57 | 0.82 | 25 | empty |
| 5 | 140 | 0.53 | 0.80 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 4886 Ų buried · 42 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P97438
- Elsewhere: RCSB PDB 6W7D · PDBe 6W7D · UniProt P97438
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