› 1bka

X-ray diffraction
2.4Å resolution

OXALATE-SUBSTITUTED DIFERRIC LACTOFERRIN

Released:
DOI: 10.2210/pdb1bka/pdb
PDB entry 1bka coloured by chain, front view.
PDB entry 1bka coloured by chain, side view.
PDB entry 1bka coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin.
Baker HM, Anderson BF, Brodie AM, Shongwe MS, Smith CA, Baker EN
Biochemistry 35 9007-13 (1996)
PMID: 8703903

Function and Biology Details

Biochemical function:
Biological process:
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: 691 amino acids
Theoretical weight: 76.26 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02788 (Residues: 21-710; Coverage: 100%)
Gene names: GIG12, LF, LTF
Sequence domains: Transferrin
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
Ligand FE 2 x FE
Ligand OXL 2 x OXL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 155.46Å b: 96.92Å c: 55.85Å
α: 90° β: 90° γ: 90°

Quick links

Citations

1 review citation

Lactoferrin, a Pleiotropic Protein in Health and Disease.
Mayeur et al. (2016)
14 other articles

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