1FQF
CRYSTAL STRUCTURES OF MUTANT (K296A) THAT ABOLISH THE DILYSINE INTERACTION IN THE N-LOBE OF HUMAN TRANSFERRIN
Summary for 1FQF
Entry DOI | 10.2210/pdb1fqf/pdb |
Related | 1A8E 1FQF |
Descriptor | SEROTRANSFERRIN, FE (III) ION, CARBONATE ION, ... (4 entities in total) |
Functional Keywords | iron transport, transferrin, n-lobe, iron-release, dilysine interaction, metal transport |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P02787 |
Total number of polymer chains | 1 |
Total formula weight | 36662.41 |
Authors | Nurizzo, D.,Baker, H.M.,Baker, E.N. (deposition date: 2000-09-04, release date: 2001-05-16, Last modification date: 2021-11-03) |
Primary citation | Nurizzo, D.,Baker, H.M.,He, Q.Y.,MacGillivray, R.T.,Mason, A.B.,Woodworth, R.C.,Baker, E.N. Crystal structures and iron release properties of mutants (K206A and K296A) that abolish the dilysine interaction in the N-lobe of human transferrin. Biochemistry, 40:1616-1623, 2001 Cited by PubMed: 11327820DOI: 10.1021/bi002050m PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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