› 2zz9

Electron crystallography
2.8Å resolution

Structure of aquaporin-4 S180D mutant at 2.8 A resolution by electron crystallography

Released:
DOI: 10.2210/pdb2zz9/pdb
PDB entry 2zz9 coloured by chain, front view.
PDB entry 2zz9 coloured by chain, side view.
PDB entry 2zz9 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Mechanism of aquaporin-4's fast and highly selective water conduction and proton exclusion.
Tani K, Mitsuma T, Hiroaki Y, Kamegawa A, Nishikawa K, Tanimura Y, Fujiyoshi Y
J Mol Biol 389 694-706 (2009)
PMID: 19406128

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-155662 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaporin-4 Chain: A
Molecule details ›
Chain: A
Length: 301 amino acids
Theoretical weight: 32.22 KDa
Source organism: Rattus norvegicus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P47863 (Residues: 23-323; Coverage: 93%)
Gene name: Aqp4
Sequence domains: Major intrinsic protein
Structure domains: Glycerol uptake facilitator protein.

Ligands and Environments

1 bound ligand:
Ligand PEE 5 x PEE
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.8Å
Expression system: Spodoptera frugiperda

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Citations

25 review citations

Physiological roles of aquaporin-4 in brain.
Nagelhus et al. (2013)
24 more

10 mentions without citation

Tuning microbial hosts for membrane protein production.
Freigassner et al. (2009)
9 more