› 1b0l

X-ray diffraction
2.2Å resolution

RECOMBINANT HUMAN DIFERRIC LACTOFERRIN

Released:
DOI: 10.2210/pdb1b0l/pdb
PDB entry 1b0l coloured by chain, front view.
PDB entry 1b0l coloured by chain, side view.
PDB entry 1b0l coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of recombinant human lactoferrin expressed in Aspergillus awamori.
Sun XL, Baker HM, Shewry SC, Jameson GB, Baker EN
Acta Crystallogr D Biol Crystallogr 55 403-7 (1999)
PMID: 10089347

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136228 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactotransferrin Chain: A
Molecule details ›
Chain: A
Length: 691 amino acids
Theoretical weight: 76.29 KDa
Source organism: Homo sapiens
Expression system: Aspergillus awamori
UniProt:
  • Canonical: P02788 (Residues: 20-710; Coverage: 100%)
Gene names: GIG12, LF, LTF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand FE 2 x FE
Ligand CO3 2 x CO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 156.25Å b: 97.53Å c: 55.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 not available 0.274
Expression system: Aspergillus awamori

Quick links

Citations

8 review citations

Helicobacter pylori persistence: an overview of interactions between H. pylori and host immune defenses.
Algood et al. (2006)
7 more

18 mentions without citation

Lactoferrin's Anti-Cancer Properties: Safety, Selectivity, and Wide Range of Action.
Cutone et al. (2020)
17 more