1cyo
From Proteopedia
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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 HEM as ligand. This structure superseeds 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
Page seeded by OCA on Tue Nov 20 12:51:27 2007
