› 4oqo

X-ray diffraction
2.42Å resolution

Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution

Released:
DOI: 10.2210/pdb4oqo/pdb
PDB 4oqo coloured by chain and viewed from the front.
PDB 4oqo coloured by chain and viewed from the side.
PDB 4oqo coloured by chain and viewed from the top.
Source organism: Bos taurus
Primary publication:
Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut.
Rastogi N, Singh A, Pandey SN, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP
FEBS J. 281 2871-82 (2014)
PMID: 24798798

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lactotransferrin Chains: A, B
Molecule details ›
Chains: A, B
Length: 348 amino acids
Theoretical weight: 38.03 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P24627 (Residues: 361-708; Coverage: 51%)
Gene name: LTF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 3 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 75.81Å b: 49.44Å c: 97.86Å
α: 90° β: 94.33° γ: 90°
R-values:
R R work R free
0.225 0.223 0.26

Quick links

Citations

1 review citation

A role for whey-derived lactoferrin and immunoglobulins in the attenuation of obesity-related inflammation and disease.
Brimelow et al. (2017)
1 other article