› 8h1d

Solid-state NMR

Solid-state NMR Structure of Aquaporin Z in its Native Cellular Membranes

Released:
DOI: 10.2210/pdb8h1d/pdb
PDB entry 8h1d coloured by chain, ensemble of 10 models, front view.
PDB entry 8h1d coloured by chain, ensemble of 10 models, side view.
PDB entry 8h1d coloured by chain, ensemble of 10 models, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Solid-state NMR structure determination of a membrane protein in E. coli cellular inner membrane.
Xie H, Zhao Y, Zhao W, Chen Y, Liu M, Yang J
OpenAccess logo Sci Adv 9 eadh4168 (2023)
PMID: 37910616

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-158106 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aquaporin Z Chain: A
Molecule details ›
Chain: A
Length: 243 amino acids
Theoretical weight: 25.19 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P60844 (Residues: 1-231; Coverage: 100%)
Gene names: JW0859, aqpZ, b0875, bniP
Sequence domains: Major intrinsic protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 36%
Refinement method: distance geometry
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Progress, Challenges and Opportunities of NMR and XL-MS for Cellular Structural Biology.
Zhang et al. (2024)

1 mention without citation

Functional regulation of aquaporin dynamics by lipid bilayer composition.
Nguyen et al. (2024)