1h76
From Proteopedia
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THE CRYSTAL STRUCTURE OF DIFERRIC PORCINE SERUM TRANSFERRIN
Overview
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 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]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 16:12:50 2007
Categories: Ferritin and Transferrin | Serum Albumin | Single protein | Sus scrofa | Bailey, S. | Hadden, J. | Hall, D.R. | Leonard, G.A. | Lindley, P.F. | Neu, M. | Winn, M. | CO3 | FE | NAG | Glycoprotein | Iron transport | Metal-binding
