› 1b8e

X-ray diffraction
1.95Å resolution

HIGH RESOLUTION CRYSTAL STRUCTURE OF THE BOVINE BETA-LACTOGLOBULIN (ISOFORMS A AND B) IN ORTHOROMBIC SPACE GROUP

Released:
DOI: 10.2210/pdb1b8e/pdb
PDB entry 1b8e coloured by chain, front view.
PDB entry 1b8e coloured by chain, side view.
PDB entry 1b8e coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition.
Oliveira KM, Valente-Mesquita VL, Botelho MM, Sawyer L, Ferreira ST, Polikarpov I
Eur J Biochem 268 477-83 (2001)
PMID: 11168385

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136154 (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: LNLS BEAMLINE D03B-MX1
Spacegroup: C2221
Unit cell:
a: 55.64Å b: 81.65Å c: 66.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.252

Quick links

Citations

1 review citation

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

8 mentions without citation

Secondary-structure analysis of denatured proteins by vacuum-ultraviolet circular dichroism spectroscopy.
Matsuo et al. (2007)
7 more