› 1vfd

X-ray diffraction
2.5Å resolution

HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY GLU (R121E)

Released:
DOI: 10.2210/pdb1vfd/pdb
PDB entry 1vfd coloured by chain, front view.
PDB entry 1vfd coloured by chain, side view.
PDB entry 1vfd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mutation of arginine 121 in lactoferrin destabilizes iron binding by disruption of anion binding: crystal structures of R121S and R121E mutants.
Faber HR, Baker CJ, Day CL, Tweedie JW, Baker EN
Biochemistry 35 14473-9 (1996)
PMID: 8931543

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: 330 amino acids
Theoretical weight: 36.59 KDa
Source organism: Homo sapiens
Expression system: Cricetinae
UniProt:
  • Canonical: P02788 (Residues: 20-349; 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
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2221
Unit cell:
a: 98.1Å b: 78.9Å c: 113.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.31
Expression system: Cricetinae

Quick links

Citations

2 review citations

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