1xfi

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(New page: 200px<br /><applet load="1xfi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xfi, resolution 1.70&Aring;" /> '''X-ray structure of g...)
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Revision as of 03:55, 21 November 2007


1xfi, resolution 1.70Å

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X-ray structure of gene product from Arabidopsis thaliana At2g17340

Overview

The crystal structure of the At2g17340 protein from A. thaliana was, determined by the multiple-wavelength anomalous diffraction method and was, refined to an R factor of 16.9% (Rfree = 22.1%) at 1.7 A resolution., At2g17340 is a member of the Pfam01937.11 protein family and its structure, provides the first insight into the structural organization of this, family. A number of fully and highly conserved residues defined by, multiple sequence alignment of members of the Pfam01937.11 family were, mapped onto the structure of At2g17340. The fully conserved residues are, involved in the coordination of a metal ion and in the stabilization of, loops surrounding the metal site. Several additional highly conserved, residues also map into the vicinity of the metal-binding site, while, others are clearly involved in stabilizing the hydrophobic core of the, protein. The structure of At2g17340 represents a new fold in protein, conformational space.

About this Structure

1XFI is a Single protein structure of sequence from Arabidopsis thaliana with MG as ligand. Full crystallographic information is available from OCA.

Reference

The structure at 1.7 A resolution of the protein product of the At2g17340 gene from Arabidopsis thaliana., Bitto E, Bingman CA, Allard ST, Wesenberg GE, Phillips GN Jr, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt, 7):630-5. Epub 2005 Jun 23. PMID:16511115

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