1D3K
HUMAN SERUM TRANSFERRIN
Summary for 1D3K
Entry DOI | 10.2210/pdb1d3k/pdb |
Related | 1A8E 1A8F 1D4N |
Descriptor | SERUM TRANSFERRIN, CARBONATE ION, FE (III) ION, ... (4 entities in total) |
Functional Keywords | iron transport, glycoprotein, transferrin, nlobe, iron-release, carbonate, metal transport |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P02787 |
Total number of polymer chains | 1 |
Total formula weight | 36523.22 |
Authors | Yang, H.-W.,MacGillivray, R.T.A.,Chen, J.,Luo, Y.,Wang, Y.,Brayer, G.D.,Mason, A.,Woodworth, R.C.,Murphy, M.E.P. (deposition date: 1999-09-29, release date: 2000-03-01, Last modification date: 2024-11-13) |
Primary citation | Yang, A.H.,MacGillivray, R.T.,Chen, J.,Luo, Y.,Wang, Y.,Brayer, G.D.,Mason, A.B.,Woodworth, R.C.,Murphy, M.E. Crystal structures of two mutants (K206Q, H207E) of the N-lobe of human transferrin with increased affinity for iron. Protein Sci., 9:49-52, 2000 Cited by PubMed Abstract: The X-ray crystallographic structures of two mutants (K206Q and H207E) of the N-lobe of human transferrin (hTF/2N) have been determined to high resolution (1.8 and 2.0 A, respectively). Both mutant proteins bind iron with greater affinity than native hTF/2N. The structures of the K206Q and H207E mutants show interactions (both H-bonding and electrostatic) that stabilize the interaction of Lys296 in the closed conformation, thereby stabilizing the iron bound forms. PubMed: 10739246PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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