Human KCC1 structure determined in kcl and lipid nanodisc

Structure

electron microscopy · 1 distinct chain · 62% helix, 4% strand (DSSP).

Ligands and binding sites

• DU0 · 2-[2-[(1~{S},2~{S},4~{S},5'~{R},6~{R},7~{S},8~{R}, 9~{S},12~{S},13~{R},16~{S})-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4, 8}.0^{13,18}]icos-18-ene-6,2'-oxane]-16-yl]oxyethyl]propane-1,3-diol · ligand · 2 copies · chains A, B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
• BGC · beta-D-glucopyranose · sugar · 4 copies · chains A, B
• GLC · alpha-D-glucopyranose · sugar · 4 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

13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1565 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

• 6KKT · human KCC1 structure determined in KCl and lipid nanodisc · the same entry in another collection · chain A against A, TM-score 1.00
• Q9UP95 · AlphaFold monomer V2.0 prediction for solute carrier family 12 member 4 (Q9UP95) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9UP95
• Elsewhere: RCSB PDB 6KKT · PDBe 6KKT · UniProt Q9UP95