› 1bsq

X-ray diffraction
2.22Å resolution

STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF POINT MUTATIONS OF VARIANTS A AND B OF BOVINE BETA-LACTOGLOBULIN

Released:
DOI: 10.2210/pdb1bsq/pdb
PDB entry 1bsq coloured by chain, front view.
PDB entry 1bsq coloured by chain, side view.
PDB entry 1bsq coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin.
Qin BY, Bewley MC, Creamer LK, Baker EN, Jameson GB
Protein Sci 8 75-83 (1999)
PMID: 10210185

Function and Biology Details

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

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
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 54.231Å b: 54.231Å c: 113.019Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.239 0.286

Quick links

Citations

3 review citations

Bovine β-lactoglobulin/fatty acid complexes: binding, structural, and biological properties.
Le Maux et al. (2014)
2 more

8 mentions without citation

Covalent cross-linking of glutathione and carnosine to proteins by 4-oxo-2-nonenal.
Zhu et al. (2009)
7 more