6lsc

X-ray diffraction
3.21Å resolution

Structure of the E202Y mutant of the Cl-/H+ antiporter CLC-ec1 from E.coli: a re-refined model of the 4FTP model

Released:
Source organism: Escherichia coli K-12
Primary publication:
Intracellular proton access in a Cl(-)/H(+) antiporter.
PLoS Biol. 10 e1001441- (2012)

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-153303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
H(+)/Cl(-) exchange transporter ClcA Chain: A
Molecule details ›
Chain: A
Length: 465 amino acids
Theoretical weight: 49.69 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P37019 (Residues: 1-465; Coverage: 98%)
Gene names: JW5012, b0155, clcA, eriC, yadQ
Sequence domains: Voltage gated chloride channel

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 90.702Å b: 85.166Å c: 100.092Å
α: 90° β: 102.61° γ: 90°
R-values:
R R work R free
0.213 0.21 0.263
Expression system: Escherichia coli K-12