› 1bsy

X-ray diffraction
2.24Å resolution

STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 7.1

Released:
DOI: 10.2210/pdb1bsy/pdb
PDB entry 1bsy coloured by chain, front view.
PDB entry 1bsy coloured by chain, side view.
PDB entry 1bsy coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural basis of the Tanford transition of bovine beta-lactoglobulin.
Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB
Biochemistry 37 14014-23 (1998)
PMID: 9760236

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: 18.39 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 RUH2R
Spacegroup: P3221
Unit cell:
a: 53.96Å b: 53.96Å c: 112.41Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.234 0.279

Quick links

Citations

19 review citations

Invited review: beta-lactoglobulin: binding properties, structure, and function.
Kontopidis et al. (2004)
18 more

18 mentions without citation

Transient non-native helix formation during the folding of β-lactoglobulin.
Ikeguchi M. (2014)
17 more