› 4gxg

X-ray diffraction
2.4Å resolution

Crystal structure of human GLTP bound with 12:0 monosulfatide (orthorhombic form; four subunits in asymmetric unit)

Released:
DOI: 10.2210/pdb4gxg/pdb
PDB entry 4gxg coloured by chain, front view.
PDB entry 4gxg coloured by chain, side view.
PDB entry 4gxg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into lipid-dependent reversible dimerization of human GLTP.
Samygina VR, Ochoa-Lizarralde B, Popov AN, Cabo-Bilbao A, Goni-de-Cerio F, Molotkovsky JG, Patel DJ, Brown RE, Malinina L
Acta Crystallogr D Biol Crystallogr 69 603-16 (2013)
PMID: 23519669

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycolipid transfer protein Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 209 amino acids
Theoretical weight: 23.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NZD2 (Residues: 1-209; Coverage: 100%)
Gene name: GLTP
Sequence domains: Glycolipid transfer protein (GLTP)
Structure domains: Glycolipid transfer protein

Ligands and Environments

1 bound ligand:
Ligand EIS 4 x EIS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 65.205Å b: 84.654Å c: 171.876Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.271
Expression system: Escherichia coli

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Citations

3 review citations

Emerging roles for human glycolipid transfer protein superfamily members in the regulation of autophagy, inflammation, and cell death.
Mishra et al. (2020)
2 more

1 mention without citation

Structural insights into lipid-dependent reversible dimerization of human GLTP.
Samygina et al. (2013)