› 6rwr

X-ray diffraction
2.1Å resolution

Engineered beta-lactoglobulin: variant M107L in complex with myristic acid

Released:
DOI: 10.2210/pdb6rwr/pdb
PDB 6rwr coloured by chain and viewed from the front.
PDB 6rwr coloured by chain and viewed from the side.
PDB 6rwr coloured by chain and viewed from the top.
Source organism: Bos taurus
Primary publication:
Structure-based design approach to rational site-directed mutagenesis of β-lactoglobulin.
Bonarek P, Loch JI, Tworzydło M, Cooper DR, Milto K, Wróbel P, Kurpiewska K, Lewiński K
J Struct Biol 210 107493 (2020)
PMID: 32169624

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactoglobulin Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 18.21 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P02754 (Residues: 17-178; Coverage: 100%)
Gene name: LGB
Sequence domains: Lipocalin / cytosolic fatty-acid binding protein family

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: Agilent SuperNova
Spacegroup: P3221
Unit cell:
a: 53.182Å b: 53.182Å c: 112.285Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.174 0.221
Expression system: Escherichia coli

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Citations

1 review citation

Milk Processing Affects Structure, Bioavailability and Immunogenicity of β-lactoglobulin.
Broersen K. (2020)