› 2b6p

X-ray diffraction
2.4Å resolution

X-ray structure of lens Aquaporin-0 (AQP0) (lens MIP) in an open pore state

Released:
DOI: 10.2210/pdb2b6p/pdb
PDB entry 2b6p coloured by chain, front view.
PDB entry 2b6p coloured by chain, side view.
PDB entry 2b6p coloured by chain, top view.
Source organism: Bos taurus
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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139107 (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: 28.24 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P06624 (Residues: 1-263; Coverage: 100%)
Gene name: MIP
Sequence domains: Major intrinsic protein
Structure domains: Glycerol uptake facilitator protein.

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P4212
Unit cell:
a: 109.531Å b: 109.531Å c: 52.822Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.242 0.292

Quick links

Citations

137 review citations

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

20 mentions without citation

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