› 6ghh

X-ray diffraction
1.9Å resolution

Thermodynamic, Crystallographic and Computational Studies of Non Mammalian Fatty Acid Binding to Bovine b-Lactoglobulin

Released:
DOI: 10.2210/pdb6ghh/pdb
PDB entry 6ghh coloured by chain, front view.
PDB entry 6ghh coloured by chain, side view.
PDB entry 6ghh coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Thermodynamic, crystallographic and computational studies of non-mammalian fatty acid binding to bovine β-Lactoglobulin.
Rovoli M, Thireou T, Choiset Y, Haertlé T, Sawyer L, Eliopoulos E, Kontopidis G
Int J Biol Macromol 118 296-303 (2018)
PMID: 29879410

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136153 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactoglobulin Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 18.3 KDa
Source organism: Bos taurus
Expression system: Bos taurus
UniProt:
  • Canonical: P02754 (Residues: 17-178; Coverage: 100%)
Gene name: LGB
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
Ligand TDA 1 x TDA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION NOVA
Spacegroup: P3221
Unit cell:
a: 53.588Å b: 53.588Å c: 111.607Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.197 0.248
Expression system: Bos taurus

Quick links

Citations

1 review citation

β-Lactoglobulin and Glycodelin: Two Sides of the Same Coin?
Sawyer L. (2021)