› 7smp

Electron Microscopy
3.28Å resolution

CryoEM structure of NKCC1 Bu-I

Released:
DOI: 10.2210/pdb7smp/pdb
PDB entry 7smp coloured by chain, front view.
PDB entry 7smp coloured by chain, side view.
PDB entry 7smp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Inhibition mechanism of NKCC1 involves the carboxyl terminus and long-range conformational coupling.
Moseng MA, Su CC, Rios K, Cui M, Lyu M, Glaza P, Klenotic PA, Delpire E, Yu EW
Sci Adv 8 eabq0952 (2022)
PMID: 36306358
Related structures: EMD-25204

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157148 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Solute carrier family 12 member 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 930 amino acids
Theoretical weight: 103.31 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P55011 (Residues: 283-1211; Coverage: 77%)
Gene names: NKCC1, SLC12A2
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand 82U 3 x 82U
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.28Å
Relevant EMDB volumes: EMD-25204
Expression system: Homo sapiens

Quick links

Citations

2 review citations

Structural Pharmacology of Cation-Chloride Cotransporters.
Zhao et al. (2022)
1 more

1 mention without citation

Technical Comment on "Inhibition mechanism of NKCC1 involves the carboxyl terminus and long-range conformational coupling".
Flygaard et al. (2023)