1cyo

<table><tr><td colspan='2'>[[1cyo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3b5c 3b5c], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2b5c 2b5c] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1b5c 1b5c]. The October 2011 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''PDB Pioneers'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2011_10 10.2210/rcsb_pdb/mom_2011_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CYO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>

[[https://www.uniprot.org/uniprot/CYB5_BOVIN CYB5_BOVIN]] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15299727</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Bovin]]

[[Category: Durley, R C.E]]

[[Category: Mathews, F S]]

[[Category: Electron transport]]