› 6vw9

X-ray diffraction
1.8Å resolution

C-terminal regulatory domain of the chloride transporter KCC-1 from C. elegans, proteolyzed during crystallization

Released:
DOI: 10.2210/pdb6vw9/pdb
PDB 6vw9 coloured by chain and viewed from the front.
PDB 6vw9 coloured by chain and viewed from the side.
PDB 6vw9 coloured by chain and viewed from the top.
Source organism: Caenorhabditis elegans
Primary publication:
Structure of the Regulatory Cytosolic Domain of a Eukaryotic Potassium-Chloride Cotransporter.
Zimanyi CM, Guo M, Mahmood A, Hendrickson WA, Hirsh D, Cheung J
Structure 28 1051-1060.e4 (2020)
PMID: 32679039

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
K+/Cl-Cotransporter Chain: A
Molecule details ›
Chain: A
Length: 233 amino acids
Theoretical weight: 26.44 KDa
Source organism: Caenorhabditis elegans
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: S6FCX2 (Residues: 661-892; Coverage: 22%)
Gene names: CELE_R13A1.2, R13A1.2, kcc-1
Sequence domains: Solute carrier family 12
K+/Cl-Cotransporter Chain: B
Molecule details ›
Chain: B
Length: 71 amino acids
Theoretical weight: 8.11 KDa
Source organism: Caenorhabditis elegans
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: S6FCX2 (Residues: 996-1066; Coverage: 7%)
Gene names: CELE_R13A1.2, R13A1.2, kcc-1
Sequence domains: Solute carrier family 12

Ligands and Environments

2 bound ligands:
Ligand P33 1 x P33
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 104.32Å b: 65.546Å c: 56.523Å
α: 90° β: 97.174° γ: 90°
R-values:
R R work R free
0.184 0.183 0.214
Expression system: Spodoptera frugiperda

Quick links

Citations

1 review citation

Implications of AlphaFold2 for crystallographic phasing by molecular replacement.
McCoy et al. (2022)
3 other articles