Research workbench
C-terminal regulatory domain of the chloride transporter kcc-1 from C. elegans, proteolyzed during crystallization
Analyse C-terminal regulatory domain of the chloride transporter kcc-1 from C. elegans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VW9
- Type
- protein
- Length
- 299 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- K+/CL-cotransporter
- UniProt
- S6FCX2
- Pockets
- 5 · best druggability 0.66
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | K+/CL-cotransporter | protein | 231 | 39% helix, 24% strand | S6FCX2 |
| B | K+/CL-cotransporter | protein | 68 | 44% helix, 15% strand | S6FCX2 |
Ligands and binding sites
- GOL · Glycerol · additive · 3 copies · chains A, B
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.66 | 0.83 | 29 | GOL |
| 2 | 87 | 0.45 | 0.80 | 18 | empty |
| 3 | 72 | 0.42 | 0.80 | 22 | empty |
| 4 | 87 | 0.35 | 0.75 | 21 | empty |
| 5 | 63 | 0.29 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 2197 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 6VW9 · C-terminal regulatory domain of the chloride transporter KCC-1 from C. elegans… · 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
- Every structure of UniProt S6FCX2
- Elsewhere: RCSB PDB 6VW9 · PDBe 6VW9 · UniProt S6FCX2
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