2cdv
From Proteopedia
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| - | [[Image:2cdv.gif|left|200px]] | + | [[Image:2cdv.gif|left|200px]] |
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| - | '''REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 2cdv |SIZE=350|CAPTION= <scene name='initialview01'>2cdv</scene>, resolution 1.8Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''REFINED STRUCTURE OF CYTOCHROME C3 AT 1.8 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CDV is a [ | + | 2CDV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Desulfovibrio_vulgaris Desulfovibrio vulgaris]. This structure supersedes the now removed PDB entry 1CDV. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CDV OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/6319712 6319712] |
[[Category: Desulfovibrio vulgaris]] | [[Category: Desulfovibrio vulgaris]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: heme protein of electron transport]] | [[Category: heme protein of electron transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:14:09 2008'' |
Revision as of 14:14, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About 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.
Reference
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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