› 1ih5

Electron crystallography
3.7Å resolution

CRYSTAL STRUCTURE OF AQUAPORIN-1

Released:
DOI: 10.2210/pdb1ih5/pdb
PDB entry 1ih5 coloured by chain, front view.
PDB entry 1ih5 coloured by chain, side view.
PDB entry 1ih5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Visualization of a water-selective pore by electron crystallography in vitreous ice.
Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK
Proc Natl Acad Sci U S A 98 1398-403 (2001)
PMID: 11171962

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-151591 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaporin-1 Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 28.55 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P29972 (Residues: 1-269; Coverage: 100%)
Gene names: AQP1, CHIP28
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
Resolution: 3.7Å

Quick links

Citations

33 review citations

Aquaporin water channels--from atomic structure to clinical medicine.
Agre et al. (2002)
32 more

13 mentions without citation

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