› 1i6q

X-ray diffraction
2.7Å resolution

Formation of a protein intermediate and its trapping by the simultaneous crystallization process: Crystal structure of an iron-saturated intermediate in the FE3+ binding pathway of camel lactoferrin at 2.7 resolution

Released:
DOI: 10.2210/pdb1i6q/pdb
PDB entry 1i6q coloured by chain, front view.
PDB entry 1i6q coloured by chain, side view.
PDB entry 1i6q coloured by chain, top view.
Source organism: Camelus dromedarius
Primary publication:
Protein intermediate trapped by the simultaneous crystallization process. Crystal structure of an iron-saturated intermediate in the Fe3+ binding pathway of camel lactoferrin at 2.7 a resolution.
Khan JA, Kumar P, Srinivasan A, Singh TP
J Biol Chem 276 36817-23 (2001)
PMID: 11473113

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-193582 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lactotransferrin Chain: A
Molecule details ›
Chain: A
Length: 689 amino acids
Theoretical weight: 75.45 KDa
Source organism: Camelus dromedarius
UniProt:
  • Canonical: Q9TUM0 (Residues: 20-708; Coverage: 100%)
Gene name: 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: C2
Unit cell:
a: 175.91Å b: 80.62Å c: 56.29Å
α: 90° β: 92.37° γ: 90°
R-values:
R R work R free
0.22 0.188 0.255

Quick links

Citations

1 review citation

Transferrin as a model system for method development to study structure, dynamics and interactions of metalloproteins using mass spectrometry.
Kaltashov et al. (2012)
9 other articles

1 mention without citation

Elucidation of molecular interactions of theaflavin monogallate with camel milk lactoferrin: detailed spectroscopic and dynamic simulation studies.
Khan et al. (2021)