› 1vfe

X-ray diffraction
2.3Å resolution

HUMAN LACTOFERRIN, N-TERMINAL LOBE MUTANT WITH ARG 121 REPLACED BY SER (R121S)

Released:
DOI: 10.2210/pdb1vfe/pdb
PDB entry 1vfe coloured by chain, front view.
PDB entry 1vfe coloured by chain, side view.
PDB entry 1vfe 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: 333 amino acids
Theoretical weight: 36.95 KDa
Source organism: Homo sapiens
Expression system: Cricetinae
UniProt:
  • Canonical: P02788 (Residues: 20-352; 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: RIGAKU RUH2R
Spacegroup: C2
Unit cell:
a: 97.9Å b: 78.8Å c: 58.9Å
α: 90° β: 99.2° γ: 90°
R-values:
R R work R free
0.196 0.196 0.27
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