1afo

Solution NMR

DIMERIC TRANSMEMBRANE DOMAIN OF HUMAN GLYCOPHORIN A, NMR, 20 STRUCTURES

Released:
Source organism: Homo sapiens
Primary publication:
A transmembrane helix dimer: structure and implications.
Science 276 131-3 (1997)
PMID: 9082985

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycophorin-A Chains: A, B
Molecule details ›
Chains: A, B
Length: 40 amino acids
Theoretical weight: 4.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02724 (Residues: 81-120; Coverage: 31%)
Gene names: GPA, GYPA
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: DISTANCE GEOMETRY SIMULATED ANNEALING HYBRID
Expression system: Escherichia coli