1blf
From Proteopedia
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STRUCTURE OF DIFERRIC BOVINE LACTOFERRIN AT 2.8 ANGSTROMS RESOLUTION
Overview
The three-dimensional structure of diferric bovine lactoferrin (bLf) has, been determined by X-ray crystallography in order to investigate the, factors that influence iron binding and release by transferrins. The, structure was solved by molecular replacement, using the coordinates of, diferric human lactoferrin (hLf) as a search model, and was refined with, data to 2.8 A resolution by simulated annealing (X-PLOR) and restrained, least squares (TNT). The final model comprises 5310 protein atoms, (residues 5 to 689), 124 carbohydrate atoms (from ten monosaccharide, units, in three glycan chains), 2 Fe3+, 2 CO32- and 50 water molecules., This model gives an R-factor of 0.232 for 21440 reflections in the, resolution range 30.0 to 2.8 A. The folding of the bLf molecule is, essentially the ... [(full description)]
About this Structure
1BLF is a [Single protein] structure of sequence from [Bos taurus] with NAG, FE and CO3 as [ligands]. Structure known Active Sites: FE1 and FE2. Full crystallographic information is available from [OCA].
Reference
Three-dimensional structure of diferric bovine lactoferrin at 2.8 A resolution., Moore SA, Anderson BF, Groom CR, Haridas M, Baker EN, J Mol Biol. 1997 Nov 28;274(2):222-36. PMID:9398529
Page seeded by OCA on Tue Oct 30 14:55:48 2007
Categories: Bos taurus | Single protein | Anderson, B.F. | Baker, E.N. | Groom, C.R. | Haridas, M. | Moore, S.A. | CO3 | FE | NAG | Carbohydrate structure | Iron-binding protein | Lactoferrin | Transferrin