› 1hse

X-ray diffraction
2.2Å resolution

H253M N TERMINAL LOBE OF HUMAN LACTOFERRIN

Released:
DOI: 10.2210/pdb1hse/pdb
PDB entry 1hse coloured by chain, front view.
PDB entry 1hse coloured by chain, side view.
PDB entry 1hse coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253-->methionine mutant.
Nicholson H, Anderson BF, Bland T, Shewry SC, Tweedie JW, Baker EN
Biochemistry 36 341-6 (1997)
PMID: 9003186

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
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: 334 amino acids
Theoretical weight: 37.2 KDa
Source organism: Homo sapiens
Expression system: Cricetinae
UniProt:
  • Canonical: P02788 (Residues: 21-353; Coverage: 48%)
Gene names: GIG12, LF, LTF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand CO3 1 x CO3
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P41212
Unit cell:
a: 58.4Å b: 58.4Å c: 217.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 not available
Expression system: Cricetinae

Quick links

Citations

3 review citations

Evolution of the transferrin family: conservation of residues associated with iron and anion binding.
Lambert et al. (2005)
2 more