Research workbench
Human traak K+ channel fhieg mutant A198E in a K+ bound conductive conformation
Analyse Human traak K+ channel fhieg mutant A198E in a K+ bound conductive conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LJ5
- Type
- protein
- Length
- 1,351 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 2 of potassium channel subfamily K member 4; Anti-traak antibody 13E9 Fab…
- Ligands
- K, CA
- Pockets
- 19 · best druggability 0.72
Structure
x-ray diffraction · 5 distinct chains · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 2 of potassium channel subfamily K member 4 | protein | 253 | 75% helix, 0% strand | — |
| B | Isoform 2 of potassium channel subfamily K member 4 | protein | 255 | 76% helix, 0% strand | — |
| D, F | Anti-traak antibody 13E9 Fab fragment light chain | protein | 211 | 6% helix, 50% strand | — |
| E | Anti-traak antibody 13E9 Fab fragment heavy chain | protein | 211 | 7% helix, 51% strand | — |
| G | Anti-traak antibody 13E9 Fab fragment heavy chain | protein | 210 | 7% helix, 51% strand | — |
Ligands and binding sites
- K · Potassium ion · metal · 7 copies · chains A, B
- CA · Calcium ion · metal · 3 copies · chains A, B, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 993 | 0.72 | 0.76 | 95 | CA, K |
| 2 | 732 | 0.70 | 0.77 | 64 | K |
| 3 | 563 | 0.61 | 0.74 | 60 | empty |
| 4 | 265 | 0.57 | 0.78 | 39 | empty |
| 5 | 423 | 0.56 | 0.73 | 56 | empty |
Interfaces
12 interfaces between chains.
- A–B · 5544 Ų buried · 46 hydrogen bonds · protein-protein
- F–G · 1784 Ų buried · 16 hydrogen bonds · protein-protein
- D–E · 1764 Ų buried · 19 hydrogen bonds · protein-protein
- A–E · 477 Ų buried · 7 hydrogen bonds · protein-protein
- B–G · 474 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 7LJ5 · Human TRAAK K+ channel FHIEG mutant A198E in a K+ bound conductive conformation · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 7LJ5 · PDBe 7LJ5
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