6nkq

X-ray diffraction
2.3Å resolution

The structure of bovine beta-lactoglobulin in novel crystals grown at pH 3.8

Released:
Source organism: Bos taurus
Primary publication:
The structure of bovine β-lactoglobulin in crystals grown at pH 3.8 exhibiting novel threefold twinning.
Acta Crystallogr F Struct Biol Commun 75 640-645 (2019)
PMID: 31584012

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactoglobulin Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 178 amino acids
Theoretical weight: 19.9 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P02754 (Residues: 1-178; Coverage: 100%)
Gene name: LGB
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 65.888Å b: 114.121Å c: 140.506Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.261