› 4h0w

X-ray diffraction
2.4Å resolution

Bismuth bound human serum transferrin

Released:
DOI: 10.2210/pdb4h0w/pdb
PDB entry 4h0w coloured by chain, front view.
PDB entry 4h0w coloured by chain, side view.
PDB entry 4h0w coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe.
Yang N, Zhang H, Wang M, Hao Q, Sun H
Sci Rep 2 999 (2012)
PMID: 23256035

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136222 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serotransferrin Chain: A
Molecule details ›
Chain: A
Length: 679 amino acids
Theoretical weight: 75.3 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02787 (Residues: 20-698; Coverage: 100%)
Gene names: PRO1400, TF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

5 bound ligands:
Ligand FE 1 x FE
Ligand CO3 2 x CO3
Ligand BS3 1 x BS3
Ligand NAG 1 x NAG
Ligand NTA 1 x NTA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 73.907Å b: 90.165Å c: 111.032Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.256

Quick links

Citations

5 review citations

Current and potential applications of bismuth-based drugs.
Keogan et al. (2014)
4 more

3 mentions without citation

Iron and bismuth bound human serum transferrin reveals a partially-opened conformation in the N-lobe.
Yang et al. (2012)
2 more