› 1tfa

X-ray diffraction
1.9Å resolution

OVOTRANSFERRIN, N-TERMINAL LOBE, APO FORM

Released:
DOI: 10.2210/pdb1tfa/pdb
PDB entry 1tfa coloured by chain, front view.
PDB entry 1tfa coloured by chain, side view.
PDB entry 1tfa coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Alternative structural state of transferrin. The crystallographic analysis of iron-loaded but domain-opened ovotransferrin N-lobe.
Mizutani K, Yamashita H, Kurokawa H, Mikami B, Hirose M
J Biol Chem 274 10190-4 (1999)
PMID: 10187803

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-136235 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ovotransferrin Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 36.25 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P02789 (Residues: 23-351; Coverage: 48%)
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE M18X
Spacegroup: P6322
Unit cell:
a: 125.17Å b: 125.17Å c: 87.26Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.187 0.243

Quick links

Citations

7 review citations

Dealing with iron: common structural principles in proteins that transport iron and heme.
Baker et al. (2003)
6 more

3 mentions without citation

Relevant B cell epitopes in allergic disease.
Pomés A. (2010)
2 more