› 1afo

Solution NMR

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

Released:
DOI: 10.2210/pdb1afo/pdb
PDB entry 1afo coloured by chain, ensemble of 20 models, front view.
PDB entry 1afo coloured by chain, ensemble of 20 models, side view.
PDB entry 1afo coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
A transmembrane helix dimer: structure and implications.
MacKenzie KR, Prestegard JH, Engelman DM
Science 276 131-3 (1997)
PMID: 9082985

Function and Biology Details

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

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: 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
Sequence domains: Glycophorin A
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

Quick links

Citations

121 review citations

Membrane protein folding and stability: physical principles.
White et al. (1999)
120 more

60 mentions without citation

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