Research workbench
Human potassium-chloride co-transporter KCC4
Analyse Human potassium-chloride co-transporter KCC4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D99
- Type
- protein
- Length
- 1,782 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium-chloride co-transporter KCC4
- UniProt
- Q9Y666
- Ligands
- NAG, K, CL
- Pockets
- 20 · best druggability 0.84
Structure
electron microscopy · 1 distinct chain · 53% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Potassium-chloride co-transporter KCC4 | protein | 891 | 53% helix, 10% strand | Q9Y666 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
- K · Potassium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 253 | 0.84 | 0.96 | 57 | CL |
| 2 | 260 | 0.84 | 0.95 | 59 | CL |
| 3 | 503 | 0.77 | 0.84 | 70 | empty |
| 4 | 511 | 0.76 | 0.84 | 60 | empty |
| 5 | 492 | 0.74 | 0.83 | 51 | empty |
Interfaces
1 interface between chains.
- A–B · 3598 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).
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 Q9Y666
- Elsewhere: RCSB PDB 7D99 · PDBe 7D99 · UniProt Q9Y666
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