› 2b6o

Electron crystallography
1.9Å resolution

Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state

Released:
DOI: 10.2210/pdb2b6o/pdb
PDB entry 2b6o coloured by chain, front view.
PDB entry 2b6o coloured by chain, side view.
PDB entry 2b6o coloured by chain, top view.
Source organism: Ovis aries
Primary publication:
Lipid-protein interactions in double-layered two-dimensional AQP0 crystals.
Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, Walz T
Nature 438 633-8 (2005)
PMID: 16319884

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179806 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lens fiber major intrinsic protein Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.28 KDa
Source organism: Ovis aries
UniProt:
  • Canonical: Q6J8I9 (Residues: 1-263; Coverage: 100%)
Gene names: AQP0, MIP
Sequence domains: Major intrinsic protein
Structure domains: Glycerol uptake facilitator protein.

Ligands and Environments

1 bound ligand:
Ligand MC3 9 x MC3
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 1.9Å

Quick links

Citations

129 review citations

How cryo-EM is revolutionizing structural biology.
Bai et al. (2015)
128 more

39 mentions without citation

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