› 6poj

Solid-state NMR

STRUCTURAL REFINEMENT OF AQUAPORIN 1 VIA SSNMR

Released:
DOI: 10.2210/pdb6poj/pdb
PDB entry 6poj coloured by chain, ensemble of 10 models, front view.
PDB entry 6poj coloured by chain, ensemble of 10 models, side view.
PDB entry 6poj coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the Functionally Important Extracellular Loop C of Human Aquaporin 1 Obtained by Solid-State NMR under Nearly Physiological Conditions.
Dingwell DA, Brown LS, Ladizhansky V
J Phys Chem B 123 7700-7710 (2019)
PMID: 31411472

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151590 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaporin-1 Chain: A
Molecule details ›
Chain: A
Length: 292 amino acids
Theoretical weight: 31.24 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P29972 (Residues: 1-269; Coverage: 100%)
Gene names: AQP1, CHIP28
Sequence domains: Major intrinsic protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 37%
Refinement method: simulated annealing
Expression system: Komagataella pastoris

Quick links

Citations

2 citation in other articles

Improved Protocol for the Production of the Low-Expression Eukaryotic Membrane Protein Human Aquaporin 2 in Pichia pastoris for Solid-State NMR.
Munro et al. (2020)
1 more

1 mention without citation

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