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Figure 3
(a) The iron-binding site in the nitrilotriacetate (NTA) complex of the 18 kDa duck ovotransferrin fragment. The iron binds to the carbonate anion and to one of the tyrosine residues, Tyr194 (188 in hST numbering). The second tyrosine, Tyr95, on a connecting strand between the two domains, is some 3.8 Å away from the iron. The NTA binds tightly to the iron through the carboxyl O atoms O4 and O8; the central N atom and the third carboxylate group provide more weakly bound ligands and the Fe—O12 linkage is not included in the figure. This carboxylate group also binds to solvent molecules. (b) The electron density in a 2|Fo| − |Fc| synthesis in the vicinity of the Fe atom, contoured at the 1 r.m.s. level.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 58| Part 5| May 2002| Pages 777-783
https://doi.org/10.1107/S0907444902003724
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