Research workbench
K2P2.1 (trek-1), 1 mm K+
Analyse K2P2.1 (trek-1), 1 mm K+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6W7C
- Type
- protein
- Length
- 534 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, B7G, R16, D10, CD, K
- Pockets
- 16 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel subfamily K member 2 | protein | 263 | 76% helix, 0% strand | P97438 |
| B | Potassium channel subfamily K member 2 | protein | 271 | 75% helix, 0% strand | P97438 |
Ligands and binding sites
- D12 · Dodecane · ligand · 3 copies · chains A, B
- B7G · heptyl beta-D-glucopyranoside · ligand · 2 copies · chains A
- R16 · Hexadecane · ligand · chains A
- D10 · Decane · ligand · chains B
- CD · Cadmium ion · metal · 3 copies · chains A, B
- K · Potassium ion · metal · 3 copies · chains A, B
- OCT · N-octane · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 988 | 0.81 | 0.82 | 104 | CD |
| 2 | 58 | 0.72 | 0.97 | 18 | empty |
| 3 | 568 | 0.67 | 0.77 | 39 | K |
| 4 | 219 | 0.61 | 0.80 | 24 | empty |
| 5 | 272 | 0.56 | 0.76 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 5066 Ų buried · 43 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 6W7C · PDBe 6W7C · UniProt P97438
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