Research workbench
Human traak K+ channel mutant G158D in a K+ bound conductive conformation
Analyse Human traak K+ channel mutant G158D 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
- 7LJB
- Type
- protein
- Length
- 1,347 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
- 20 · best druggability 0.76
Structure
x-ray diffraction · 5 distinct chains · 37% 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 | 251 | 76% helix, 0% strand | — |
| D, F | Anti-traak antibody 13E9 Fab fragment light chain | protein | 211 | 7% helix, 52% 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, 50% strand | — |
Ligands and binding sites
- K · Potassium ion · metal · 6 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
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1011 | 0.76 | 0.77 | 69 | K |
| 2 | 984 | 0.72 | 0.76 | 102 | K |
| 3 | 155 | 0.68 | 0.87 | 21 | empty |
| 4 | 507 | 0.60 | 0.74 | 55 | empty |
| 5 | 433 | 0.58 | 0.75 | 60 | empty |
Interfaces
12 interfaces between chains.
- A–B · 5199 Ų buried · 45 hydrogen bonds · protein-protein
- F–G · 1788 Ų buried · 14 hydrogen bonds · protein-protein
- D–E · 1728 Ų buried · 14 hydrogen bonds · protein-protein
- B–G · 484 Ų buried · 9 hydrogen bonds · protein-protein
- A–E · 478 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
Compared structures
- 7LJB · Human TRAAK K+ channel mutant G158D 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 7LJB · PDBe 7LJB
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