› 3c02

X-ray diffraction
2.05Å resolution

X-ray structure of the aquaglyceroporin from Plasmodium falciparum

Released:
DOI: 10.2210/pdb3c02/pdb
PDB entry 3c02 coloured by chain, front view.
PDB entry 3c02 coloured by chain, side view.
PDB entry 3c02 coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Crystal structure of the aquaglyceroporin PfAQP from the malarial parasite Plasmodium falciparum.
Newby ZE, O'Connell J, Robles-Colmenares Y, Khademi S, Miercke LJ, Stroud RM
Nat Struct Mol Biol 15 619-25 (2008)
PMID: 18500352

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaglyceroporin Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 28.32 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WPZ6 (Residues: 1-258; Coverage: 100%)
Gene name: AQP
Sequence domains: Major intrinsic protein
Structure domains: Glycerol uptake facilitator protein.

Ligands and Environments

2 bound ligands:
Ligand BOG 1 x BOG
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: I422
Unit cell:
a: 92.43Å b: 92.43Å c: 193.168Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.198
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Structural insights into eukaryotic aquaporin regulation.
Törnroth-Horsefield et al. (2010)
17 more

34 mentions without citation

Aquaporins: important but elusive drug targets.
Verkman et al. (2014)
33 more