4x1b

Human serum transferrin with ferric ion bound at the C-lobe onlyHuman serum transferrin with ferric ion bound at the C-lobe only

Structural highlights 4x1b is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.45Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease TRFE_HUMAN Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:209300. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia. Function TRFE_HUMAN Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. Publication Abstract from PubMed X-ray crystal structures of human serum transferrin (77 kDa) with YbIII or FeIII bound to the C-lobe and malonate as the synergistic anion show that the large YbIII ion causes the expansion of the metal binding pocket while octahedral metal coordination geometry is preserved, an unusual geometry for a lanthanide ion. "Anion clamp" allows flexible protein to impose coordination geometry on metal ions.,Wang M, Lai TP, Wang L, Zhang H, Yang N, Sadler PJ, Sun H Chem Commun (Camb). 2015 Apr 9. PMID:25854324 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transferrin 3D structures

spinqualitylabelsall models 4x1b, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image