2fha

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File:2fha.gif


2fha, resolution 1.9Å

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HUMAN H CHAIN FERRITIN

OverviewOverview

Mammalian ferritins are 24-mers assembled from two types of polypeptide, chain which provide the molecule with different functions. H(eavy) chains, catalyse the first step in iron storage, the oxidation of iron(II)., L(ight) chains promote the nucleation of the mineral ferrihydrite enabling, storage of iron(III) inside the protein shell. We report here the, comparison of the three-dimensional structures of recombinant human H, chain (HuHF) and horse L chain (HoLF) ferritin homopolymers, which have, been refined at 1.9 A resolution. There is 53% sequence identity between, these molecules, and the two structures are very similar, the H and L, subunit alpha-carbons superposing to within 0.5 A rms deviation with 41, water molecules in common. Nevertheless, there are significant important, ... [(full description)]

About this StructureAbout this Structure

2FHA is a [Single protein] structure of sequence from [Homo sapiens] with CA as [ligand]. Structure known Active Site: FOX. Full crystallographic information is available from [OCA].

ReferenceReference

Comparison of the three-dimensional structures of recombinant human H and horse L ferritins at high resolution., Hempstead PD, Yewdall SJ, Fernie AR, Lawson DM, Artymiuk PJ, Rice DW, Ford GC, Harrison PM, J Mol Biol. 1997 May 2;268(2):424-48. PMID:9159481

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