› 1rc2

X-ray diffraction
2.5Å resolution

2.5 Angstrom Resolution X-ray Structure of Aquaporin Z

Released:
DOI: 10.2210/pdb1rc2/pdb
PDB entry 1rc2 coloured by chain, front view.
PDB entry 1rc2 coloured by chain, side view.
PDB entry 1rc2 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z.
Savage DF, Egea PF, Robles-Colmenares Y, O'Connell JD, Stroud RM
PLoS Biol 1 E72 (2003)
PMID: 14691544

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-158108 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaporin Z Chains: A, B
Molecule details ›
Chains: A, B
Length: 231 amino acids
Theoretical weight: 23.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P60844 (Residues: 1-231; Coverage: 100%)
Gene names: JW0859, aqpZ, b0875, bniP
Sequence domains: Major intrinsic protein
Structure domains: Glycerol uptake facilitator protein.

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P4
Unit cell:
a: 93.55Å b: 93.55Å c: 80.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.268
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs.
Senes et al. (2004)
26 more

79 mentions without citation

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