› 3nd0

X-ray diffraction
3.2Å resolution

X-ray crystal structure of a slow cyanobacterial Cl-/H+ antiporter

Released:
DOI: 10.2210/pdb3nd0/pdb
PDB entry 3nd0 coloured by chain, front view.
PDB entry 3nd0 coloured by chain, side view.
PDB entry 3nd0 coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803
Primary publication:
Structure of a slow CLC Cl⁻/H+ antiporter from a cyanobacterium.
Jayaram H, Robertson JL, Wu F, Williams C, Miller C
Biochemistry 50 788-94 (2011)
PMID: 21174448

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-159903 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
H(+)/Cl(-) exchange transporter ClcA Chains: A, B
Molecule details ›
Chains: A, B
Length: 466 amino acids
Theoretical weight: 50.11 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P73745 (Residues: 1-451; Coverage: 100%)
Gene name: sll0855
Sequence domains: Voltage gated chloride channel
Structure domains: Clc chloride channel

Ligands and Environments

1 bound ligand:
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P321
Unit cell:
a: 203.79Å b: 203.79Å c: 96.82Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.243 0.269
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

CLC channel function and dysfunction in health and disease.
Stölting et al. (2014)
10 more

2 mentions without citation

Glycines: role in α-helical membrane protein structures and a potential indicator of native conformation.
Dong et al. (2012)
1 more