› 2o9g

X-ray diffraction
1.9Å resolution

Crystal Structure of AqpZ mutant L170C complexed with mercury.

Released:
DOI: 10.2210/pdb2o9g/pdb
PDB entry 2o9g coloured by chain, front view.
PDB entry 2o9g coloured by chain, side view.
PDB entry 2o9g coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis of aquaporin inhibition by mercury.
Savage DF, Stroud RM
J Mol Biol 368 607-17 (2007)
PMID: 17376483

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-158108 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaporin Z Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 23.97 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

2 bound ligands:
Ligand BOG 2 x BOG
Ligand HG 4 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: I4
Unit cell:
a: 91.156Å b: 91.156Å c: 77.145Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.166 0.195
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Water channel proteins (later called aquaporins) and relatives: past, present, and future.
Benga G. (2009)
12 more

7 mentions without citation

TMPad: an integrated structural database for helix-packing folds in transmembrane proteins.
Lo et al. (2011)
6 more