› 5dye

X-ray diffraction
3.5Å resolution

CRYSTAL STRUCTURE OF THE FULL LENGTH S156E MUTANT OF HUMAN AQUAPORIN 5

Released:
DOI: 10.2210/pdb5dye/pdb
PDB entry 5dye coloured by chain, front view.
PDB entry 5dye coloured by chain, side view.
PDB entry 5dye coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Plasma Membrane Abundance of Human Aquaporin 5 Is Dynamically Regulated by Multiple Pathways.
Kitchen P, Öberg F, Sjöhamn J, Hedfalk K, Bill RM, Conner AC, Conner MT, Törnroth-Horsefield S
PLoS One 10 e0143027 (2015)
PMID: 26569106

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-157168 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaporin-5 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 265 amino acids
Theoretical weight: 28.35 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P55064 (Residues: 1-265; Coverage: 100%)
Gene name: AQP5
Sequence domains: Major intrinsic protein
Structure domains: Glycerol uptake facilitator protein.

Ligands and Environments

1 bound ligand:
Ligand PS6 1 x PS6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P312
Unit cell:
a: 174.286Å b: 174.286Å c: 100.858Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.28 0.279 0.311
Expression system: Komagataella pastoris

Quick links

Citations

17 review citations

Aquaporin-5: from structure to function and dysfunction in cancer.
Direito et al. (2016)
16 more

4 mentions without citation

Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.
Ozu et al. (2022)
3 more