2cn7: Difference between revisions

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New page: left|200px<br /> <applet load="2cn7" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cn7, resolution 1.75Å" /> '''RECOMBINANT HUMAN H...
 
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==About this Structure==
==About this Structure==
2CN7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CN7 OCA]].  
2CN7 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with CA and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.16.3.1 1.16.3.1]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CN7 OCA]].  


==Reference==
==Reference==
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[[Category: phosphorylation]]
[[Category: phosphorylation]]


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Revision as of 09:20, 30 October 2007

File:2cn7.gif


2cn7, resolution 1.75Å

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RECOMBINANT HUMAN H FERRITIN, K86Q, E27D AND E107D MUTANT

OverviewOverview

Ferritins are a family of proteins distributed widely in nature. In, bacterial, plant, and animal cells, ferritin appears to serve as a, soluble, bioavailable, and non-toxic form of iron provider. Ferritins from, animal sources are heteropolymers composed of two types of subunit, H and, L, which differ mainly by the presence (H) or absence (L) of active, ferroxidase centres. We report the crystallographic structures of four, human H apoferritin variants at a resolution of up to 1.5 Angstrom., Crystal derivatives using Zn(II) as redox-stable alternative for Fe(II), allows us to characterize the different metal-binding sites. The, ferroxidase centre, which is composed of sites A and B, binds metal with a, preference for the A site. In addition, distinct Zn(II)-binding sites were, found in ... [(full description)]

About this StructureAbout this Structure

2CN7 is a [Single protein] structure of sequence from [Homo sapiens] with CA and GOL as [ligands]. Active as [Oxidoreductase], with EC number [1.16.3.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

High-resolution X-ray structures of human apoferritin H-chain mutants correlated with their activity and metal-binding sites., Toussaint L, Bertrand L, Hue L, Crichton RR, Declercq JP, J Mol Biol. 2007 Jan 12;365(2):440-52. Epub 2006 Oct 7. PMID:17070541

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