1cyo
From Proteopedia
(New page: 200px<br /><applet load="1cyo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cyo, resolution 1.5Å" /> '''BOVINE CYTOCHROME B(5...) |
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| - | [[Image:1cyo.jpg|left|200px]]<br /><applet load="1cyo" size=" | + | [[Image:1cyo.jpg|left|200px]]<br /><applet load="1cyo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cyo, resolution 1.5Å" /> | caption="1cyo, resolution 1.5Å" /> | ||
'''BOVINE CYTOCHROME B(5)'''<br /> | '''BOVINE CYTOCHROME B(5)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of bovine liver cytochrome b(5), a soluble 93-residue | + | The structure of bovine liver cytochrome b(5), a soluble 93-residue proteolytic fragment of a 16 kDa membrane-bound hemoprotein, initially solved at 2.0 A resolution, has been refined at 1.5 A using data collected on a diffractometer. Refinement to 2.0 A resolution used the Hendrickson-Konnert procedure PROLSQ and was then extended to 1.5 A resolution using the program PROFFT. Only residues 3-87 could be identified in the model and these residues together with 93 water molecules gave an agreement factor of R = 0.161 for data in the resolution range 1.5-5 A. The structure was finally refined using the program X-PLOR, which enabled alternate conformers to be modelled for several surface side chains. Residues 1 and 2 at the amino terminus of the protein and residue 88 near the carboxyl terminus could be identified from these electron-density maps. However the remaining disordered carboxy-terminal residues could not successfully be included in the model. A total of 117 solvent molecules were included in the final refinement to give R = 0.164 for the data between 1.5 and 10 A. |
==About this Structure== | ==About this Structure== | ||
| - | 1CYO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1CYO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entries 3B5C, 2B5C and 1B5C. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Durley, R | + | [[Category: Durley, R C.E.]] |
| - | [[Category: Mathews, F | + | [[Category: Mathews, F S.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: electron transport]] | [[Category: electron transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:05 2008'' |
Revision as of 10:11, 21 February 2008
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BOVINE CYTOCHROME B(5)
Overview
The structure of bovine liver cytochrome b(5), a soluble 93-residue proteolytic fragment of a 16 kDa membrane-bound hemoprotein, initially solved at 2.0 A resolution, has been refined at 1.5 A using data collected on a diffractometer. Refinement to 2.0 A resolution used the Hendrickson-Konnert procedure PROLSQ and was then extended to 1.5 A resolution using the program PROFFT. Only residues 3-87 could be identified in the model and these residues together with 93 water molecules gave an agreement factor of R = 0.161 for data in the resolution range 1.5-5 A. The structure was finally refined using the program X-PLOR, which enabled alternate conformers to be modelled for several surface side chains. Residues 1 and 2 at the amino terminus of the protein and residue 88 near the carboxyl terminus could be identified from these electron-density maps. However the remaining disordered carboxy-terminal residues could not successfully be included in the model. A total of 117 solvent molecules were included in the final refinement to give R = 0.164 for the data between 1.5 and 10 A.
About this Structure
1CYO is a Single protein structure of sequence from Bos taurus with as ligand. This structure supersedes the now removed PDB entries 3B5C, 2B5C and 1B5C. Full crystallographic information is available from OCA.
Reference
Refinement and structural analysis of bovine cytochrome b5 at 1.5 A resolution., Durley RC, Mathews FS, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):65-76. PMID:15299727
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