› 2af9

X-ray diffraction
2Å resolution

Crystal Structure analysis of GM2-Activator protein complexed with phosphatidylcholine

Released:
DOI: 10.2210/pdb2af9/pdb
PDB entry 2af9 coloured by chain, front view.
PDB entry 2af9 coloured by chain, side view.
PDB entry 2af9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure analysis of phosphatidylcholine-GM2-activator product complexes: evidence for hydrolase activity.
Wright CS, Mi LZ, Lee S, Rastinejad F
Biochemistry 44 13510-21 (2005)
PMID: 16216074

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: 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

4 bound ligands:
Ligand OLA 1 x OLA
Ligand MYR 1 x MYR
Ligand DAO 2 x DAO
Ligand IPA 2 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 39.12Å b: 41.98Å c: 114.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.222 0.279
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Lipid transfer proteins: the lipid commute via shuttles, bridges and tubes.
Wong et al. (2019)
6 more

1 mention without citation

Applying physics-based scoring to calculate free energies of binding for single amino acid mutations in protein-protein complexes.
Beard et al. (2013)