› 1btj

X-ray diffraction
3.2Å resolution

HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE, APO FORM, CRYSTAL FORM 2

Released:
DOI: 10.2210/pdb1btj/pdb
PDB entry 1btj coloured by chain, front view.
PDB entry 1btj coloured by chain, side view.
PDB entry 1btj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin.
Jeffrey PD, Bewley MC, MacGillivray RT, Mason AB, Woodworth RC, Baker EN
Biochemistry 37 13978-86 (1998)
PMID: 9760232

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-136222 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serotransferrin Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.22 KDa
Source organism: Homo sapiens
Expression system: Cricetinae
UniProt:
  • Canonical: P02787 (Residues: 20-356; Coverage: 50%)
Gene names: PRO1400, TF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 63Å b: 77.3Å c: 72.6Å
α: 90° β: 104.3° γ: 90°
R-values:
R R work R free
0.217 0.217 0.312
Expression system: Cricetinae

Quick links

Citations

13 review citations

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

3 mentions without citation

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