› 2evs

X-ray diffraction
2.2Å resolution

Crystal structure of human Glycolipid Transfer Protein complexed with n-hexyl-beta-D-glucoside

Released:
DOI: 10.2210/pdb2evs/pdb
PDB entry 2evs coloured by chain, front view.
PDB entry 2evs coloured by chain, side view.
PDB entry 2evs 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 Chains: A, E
Molecule details ›
Chains: A, 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

3 bound ligands:
Ligand GLC 2 x GLC
Ligand HEX 3 x HEX
Ligand D10 1 x D10
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 157.913Å b: 42.18Å c: 70.819Å
α: 90° β: 104.57° γ: 90°
R-values:
R R work R free
0.192 0.19 0.236
Expression system: Escherichia coli

Quick links

Citations

12 review citations

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

2 mentions without citation

The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.
Malinina et al. (2006)
1 more