› 2kpe

Solution NMR

Refined structure of Glycophorin A transmembrane segment dimer in DPC micelles

Released:
DOI: 10.2210/pdb2kpe/pdb
PDB entry 2kpe coloured by chain, ensemble of 20 models, front view.
PDB entry 2kpe coloured by chain, ensemble of 20 models, side view.
PDB entry 2kpe coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Dimeric structure of the transmembrane domain of glycophorin a in lipidic and detergent environments.
Mineev KS, Bocharov EV, Volynsky PE, Goncharuk MV, Tkach EN, Ermolyuk YS, Schulga AA, Chupin VV, Maslennikov IV, Efremov RG, Arseniev AS
Acta Naturae 3 90-8 (2011)
PMID: 22649687

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136102 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycophorin-A Chains: A, B
Molecule details ›
Chains: A, B
Length: 29 amino acids
Theoretical weight: 3.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02724 (Residues: 89-117; Coverage: 22%)
Gene names: GPA, GYPA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

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Citations

6 review citations

Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.
Fairweather et al. (2021)
5 more

8 mentions without citation

Molecular dynamics simulations of biological membranes and membrane proteins using enhanced conformational sampling algorithms.
Mori et al. (2016)
7 more