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1D3K

HUMAN SERUM TRANSFERRIN

Summary for 1D3K
Entry DOI10.2210/pdb1d3k/pdb
Related1A8E 1A8F 1D4N
DescriptorSERUM TRANSFERRIN, CARBONATE ION, FE (III) ION, ... (4 entities in total)
Functional Keywordsiron transport, glycoprotein, transferrin, nlobe, iron-release, carbonate, metal transport
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P02787
Total number of polymer chains1
Total formula weight36523.22
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 citationYang, 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: 10739246
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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