1biy
From Proteopedia
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| - | [[Image:1biy.jpg|left|200px]]<br /><applet load="1biy" size=" | + | [[Image:1biy.jpg|left|200px]]<br /><applet load="1biy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1biy, resolution 3.37Å" /> | caption="1biy, resolution 3.37Å" /> | ||
'''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN'''<br /> | '''STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BIY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis] with FE and CO3 as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=FE1:Fe Binding Site In N-Lobe'>FE1</scene> and <scene name='pdbsite=FE2:Fe Binding Site In C-Lobe'>FE2</scene>. Full crystallographic information is available from [http:// | + | 1BIY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bubalus_bubalis Bubalus bubalis] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=CO3:'>CO3</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=FE1:Fe+Binding+Site+In+N-Lobe'>FE1</scene> and <scene name='pdbsite=FE2:Fe+Binding+Site+In+C-Lobe'>FE2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BIY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: structure]] | [[Category: structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:33:04 2008'' |
Revision as of 07:33, 3 February 2008
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STRUCTURE OF DIFERRIC BUFFALO LACTOFERRIN
Overview
The three-dimensional structure of diferric buffalo lactoferrin has been, determined at 3.3 A resolution. The structure was solved by molecular, replacement using the coordinates of diferric human lactoferrin as a, search model and was refined by simulated annealing (X-PLOR). The final, model comprises 5316 protein atoms for all 689 residues, two Fe(3+) and, two CO(3)(2-) ions. The final R factor was 21.8% for 11 711 reflections in, the resolution range 17.0-3.3 A. The folding of buffalo lactoferrin is, essentially similar to that of the other members of the transferrin, family. The significant differences are found in the dimensions of the, binding cleft and the interlobe orientation. The interlobe interactions, are predominantly hydrophobic in nature, thus facilitating the sliding of, two lobes owing to external forces. The interdomain interactions are, comparable in the N and C lobes.
About this Structure
1BIY is a Single protein structure of sequence from Bubalus bubalis with and as ligands. Known structural/functional Sites: and . Full crystallographic information is available from OCA.
Reference
Structure of buffalo lactoferrin at 3.3 A resolution at 277 K., Karthikeyan S, Yadav S, Paramasivam M, Srinivasan A, Singh TP, Acta Crystallogr D Biol Crystallogr. 2000 Jun;56(Pt 6):684-9. PMID:10818344
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