› 2euk

X-ray diffraction
1.85Å resolution

Crystal Structure of Human Glycolipid Transfer Protein complexed with 24:1 Galactosylceramide

Released:
DOI: 10.2210/pdb2euk/pdb
PDB entry 2euk coloured by chain, front view.
PDB entry 2euk coloured by chain, side view.
PDB entry 2euk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.
Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ
OpenAccess logo PLoS Biol 4 e362 (2006)
PMID: 17105344

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-192739 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycolipid transfer protein Chain: A
Molecule details ›
Chain: A
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

4 bound ligands:
Ligand GAL 1 x GAL
Ligand SPH 1 x SPH
Ligand NER 1 x NER
Ligand OCT 1 x OCT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 75.867Å b: 49.304Å c: 68.655Å
α: 90° β: 122.61° γ: 90°
R-values:
R R work R free
0.183 0.181 0.23
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Membranes in balance: mechanisms of sphingolipid homeostasis.
Breslow et al. (2010)
10 more

9 mentions without citation

How α-Helical Motifs Form Functionally Diverse Lipid-Binding Compartments.
Malinina et al. (2017)
8 more