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3mus
From Proteopedia
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{{STRUCTURE_3mus| PDB=3mus | SCENE= }} | {{STRUCTURE_3mus| PDB=3mus | SCENE= }} | ||
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===2A Resolution Structure of Rat Type B Cytochrome b5=== | ===2A Resolution Structure of Rat Type B Cytochrome b5=== | ||
| + | {{ABSTRACT_PUBMED_21574570}} | ||
| + | ==Function== | ||
| + | [[http://www.uniprot.org/uniprot/CYB5B_RAT CYB5B_RAT]] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases. | ||
==About this Structure== | ==About this Structure== | ||
[[3mus]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MUS OCA]. | [[3mus]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MUS OCA]. | ||
| - | == | + | ==Reference== |
| - | + | <ref group="xtra">PMID:021574570</ref><references group="xtra"/><references/> | |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Benson, D R.]] | [[Category: Benson, D R.]] | ||
Revision as of 07:53, 19 June 2013
Contents |
2A Resolution Structure of Rat Type B Cytochrome b5
Template:ABSTRACT PUBMED 21574570
Function
[CYB5B_RAT] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases.
About this Structure
3mus is a 2 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
- Parthasarathy S, Altuve A, Terzyan S, Zhang X, Kuczera K, Rivera M, Benson DR. Accommodating a nonconservative internal mutation by water-mediated hydrogen bonding between beta-sheet strands: a comparison of human and rat type B (mitochondrial) cytochrome b5. Biochemistry. 2011 Jun 21;50(24):5544-54. doi: 10.1021/bi2004729. Epub 2011 May, 26. PMID:21574570 doi:10.1021/bi2004729
