1h76: Difference between revisions
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THE CRYSTAL STRUCTURE OF DIFERRIC PORCINE SERUM TRANSFERRIN
OverviewOverview
The serum transferrins are monomeric proteins with a molecular mass of, around 80 kDa and are responsible for the transport of iron in, vertebrates. The three-dimensional structures of diferric porcine and, rabbit serum transferrin have been refined against X-ray diffraction data, extending to 2.15 and 2.60 A, respectively. Data for both proteins were, collected using synchrotron radiation at temperatures of 277 K. The, porcine protein crystallizes in the space group C2, with unit-cell, parameters a = 223.8, b = 44.9, c = 78.9 A, beta = 105.4 degrees with one, molecule in the asymmetric unit. The structure was solved by, molecular-replacement methods using rabbit serum transferrin as the search, model. The structure was refined using REFMAC, with a final residual of, 13.8% (R(free) = ... [(full description)]
About this StructureAbout this Structure
1H76 is a [Single protein] structure of sequence from [Sus scrofa] with NAG, CO3 and FE as [ligands]. The following pages contain interesting information on the relation of 1H76 with [Serum Albumin]. Structure known Active Site: NFE. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal and molecular structures of diferric porcine and rabbit serum transferrins at resolutions of 2.15 and 2.60 A, respectively., Hall DR, Hadden JM, Leonard GA, Bailey S, Neu M, Winn M, Lindley PF, Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):70-80. Epub 2001, Dec 21. PMID:11752780
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