PDBe 1pu5

X-ray diffraction
1.9Å resolution

GM2-activator Protein crystal structure

Released:
Source organism: Homo sapiens
Primary publication:
Structural analysis of lipid complexes of GM2-activator protein.
J. Mol. Biol. 331 951-64 (2003)
PMID: 12909021

Function and Biology Details

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ganglioside GM2 activator Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 164 amino acids
Theoretical weight: 17.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P17900 (Residues: 32-193; Coverage: 95%)
Gene name: GM2A
Sequence domains: ML domain
Structure domains: Ganglioside GM2 activator

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: P212121
Unit cell:
a: 63.32Å b: 86.13Å c: 120.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.214 0.253
Expression system: Escherichia coli BL21(DE3)