› 1r5l

X-ray diffraction
1.5Å resolution

Crystal Structure of Human Alpha-Tocopherol Transfer Protein Bound to its Ligand

Released:
DOI: 10.2210/pdb1r5l/pdb
PDB entry 1r5l coloured by chain, front view.
PDB entry 1r5l coloured by chain, side view.
PDB entry 1r5l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human alpha-tocopherol transfer protein bound to its ligand: implications for ataxia with vitamin E deficiency.
Min KC, Kovall RA, Hendrickson WA
Proc Natl Acad Sci U S A 100 14713-8 (2003)
PMID: 14657365

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-tocopherol transfer protein Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 30.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49638 (Residues: 21-278; Coverage: 93%)
Gene names: TPP1, TTPA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand VIV 1 x VIV
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P212121
Unit cell:
a: 40.096Å b: 77.151Å c: 85.397Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

31 review citations

Vitamin E, antioxidant and nothing more.
Traber et al. (2007)
30 more

13 mentions without citation

The Sec14 superfamily and mechanisms for crosstalk between lipid metabolism and lipid signaling.
Bankaitis et al. (2010)
12 more