Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
CO3 Carbonate ion
FE Fe (III) ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1A8E   PDBj   RCSB PDB   PDBe
Header : IRON TRANSPORT
Title : HUMAN SERUM TRANSFERRIN, RECOMBINANT N-TERMINAL LOBE
Release Data : 1998-06-17
Compound :
mol_id molecule chains
1 SERUM TRANSFERRIN A
fragment: N-TERMINAL LOBE
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Cricetinae  (taxid:10026)
cell_line: BABY HAMSTER KIDNEY CELLS
organ: KIDNEY
cellular_location: EXTRACELLULAR
expression_system_common: Hamsters
expression_system_vector: PNUT-BHK
Authors : Macgillivray, R.T.A., Moore, S.A., Chen, J., Anderson, B.F., Baker, H., Luo, Y., Bewley, M., Smith, C.A., Murphy, M.E.P., Wang, Y., Mason, A.B., Woodworth, R.C., Brayer, G.D., Baker, E.N.
Keywords : IRON TRANSPORT, GLYCOPROTEIN, TRANSFERRIN, NLOBE, IRON-RELEASE, CARBONATE
Exp. method : X-RAY DIFFRACTION ( 1.60 Å )
Citation :

Two high-resolution crystal structures of the recombinant N-lobe of human transferrin reveal a structural change implicated in iron release.

MacGillivray, R.T.,Moore, S.A.,Chen, J.  et al.
(1998)  Biochemistry  37 : 7919 - 7928

PubMed: 9609685
DOI: 10.1021/bi980355j

Chain : A
UniProt : P02787 (TRFE_HUMAN)
Reaction : -