› 6ada

X-ray diffraction
3.15Å resolution

Crystal structure of the E148D mutant CLC-ec1 in 200mM bromide

Released:
DOI: 10.2210/pdb6ada/pdb
PDB entry 6ada coloured by chain, front view.
PDB entry 6ada coloured by chain, side view.
PDB entry 6ada coloured by chain, top view.
Source organisms:
Primary publication:
Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC Cl-/H+ antiporter.
Park K, Lee BC, Lim HH
Proc Natl Acad Sci U S A 116 17345-17354 (2019)
PMID: 31409705

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-211161 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
H(+)/Cl(-) exchange transporter ClcA Chains: A, B
Molecule details ›
Chains: A, B
Length: 473 amino acids
Theoretical weight: 50.38 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P37019 (Residues: 1-473; Coverage: 100%)
Gene names: JW5012, b0155, clcA, eriC, yadQ
Sequence domains: Voltage gated chloride channel
antibody Fab fragment, heavy chain Chains: C, E
Molecule details ›
Chains: C, E
Length: 222 amino acids
Theoretical weight: 23.82 KDa
Source organism: Mus musculus
antibody Fab fragment, light chain Chains: D, F
Molecule details ›
Chains: D, F
Length: 211 amino acids
Theoretical weight: 23.09 KDa
Source organism: Mus musculus

Ligands and Environments

1 bound ligand:
Ligand BR 4 x BR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: C2
Unit cell:
a: 232.409Å b: 99.956Å c: 170.811Å
α: 90° β: 131.88° γ: 90°
R-values:
R R work R free
0.234 0.231 0.29
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The challenges and prospects of Escherichia coli as an organic acid production host under acid stress.
Yang et al. (2021)
6 other articles

1 mention without citation

Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC Cl-/H+ antiporter.
Park et al. (2019)