2cdv: Difference between revisions

Revision as of 07:44, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2cdv.png

Template:STRUCTURE 2cdv

REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTIONREFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 6319712

About this StructureAbout this Structure

2CDV is a Single protein structure of sequence from Desulfovibrio vulgaris. This structure supersedes the now removed PDB entry 1cdv. Full crystallographic information is available from OCA.

ReferenceReference

Refined structure of cytochrome c3 at 1.8 A resolution., Higuchi Y, Kusunoki M, Matsuura Y, Yasuoka N, Kakudo M, J Mol Biol. 1984 Jan 5;172(1):109-39. PMID:6319712

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OCA

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-'''REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION'''
+===REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION===
-==Overview==
+<!--
-The structure of cytochrome c3 from the sulfate-reducing bacterium Desulfovibrio vulgaris Miyazaki has been successfully refined at 1.8 A resolution. The crystallographic R factor is 0.176 for 9907 significant reflections. The isotropic temperature factors of individual atoms were refined and a total of 47 water molecules located on the difference map were incorporated in the refinement. The four heme groups are closely packed, with adjacent pairs of heme planes being nearly perpendicular to each other. The fifth and the sixth ligands of the heme iron atoms are histidine residues with N epsilon 2-Fe distances ranging from 1.88 A to 2.12 A. The histidine co-ordination to the heme iron is different for each heme group. The heme groups are all highly exposed to solvent, although the actual regions exposed differ among the hemes. The four heme groups are located in different environments, and the heme planes are deformed from planarity. The differences in the heme structures and their environments indicate that the four heme groups are non-equivalent. The chemical as well as the physical properties of cytochrome c3 should be interpreted in terms of the structural non-equivalence of the heme groups. The characteristic secondary structural non-equivalence of the heme groups. The characteristic secondary structures of the polypeptide chain of this molecule are three short alpha-helices, two short beta-strands and ten reverse turns.
+The line below this paragraph, {{ABSTRACT_PUBMED_6319712}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 6319712 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_6319712}}
 ==About this Structure==
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 [[Category: Yasuoka, N.]]
 [[Category: Heme protein of electron transport]]
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