› 1pub

X-ray diffraction
2.51Å resolution

GM2-activator Protein crystal structure

Released:
DOI: 10.2210/pdb1pub/pdb
PDB entry 1pub coloured by chain, front view.
PDB entry 1pub coloured by chain, side view.
PDB entry 1pub coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of lipid complexes of GM2-activator protein.
Wright CS, Zhao Q, Rastinejad F
J Mol Biol 331 951-64 (2003)
PMID: 12909021

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148206 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ganglioside GM2 activator Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 17.6 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:
Ligand 3PH 1 x 3PH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 40.07Å b: 42.42Å c: 113.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.286
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

18 review citations

Principles of lysosomal membrane digestion: stimulation of sphingolipid degradation by sphingolipid activator proteins and anionic lysosomal lipids.
Kolter et al. (2005)
17 more

6 mentions without citation

The role of hydrophobic interactions in positioning of peripheral proteins in membranes.
Lomize et al. (2007)
5 more