3ner: Difference between revisions

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[[Image:3ner.png|left|200px]]
{{STRUCTURE_3ner|  PDB=3ner  |  SCENE=  }}  
{{STRUCTURE_3ner|  PDB=3ner  |  SCENE=  }}  
===Structure of Human Type B Cytochrome b5===
===Structure of Human Type B Cytochrome b5===
{{ABSTRACT_PUBMED_21574570}}


==Function==
[[http://www.uniprot.org/uniprot/CYB5B_HUMAN CYB5B_HUMAN]] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases (By similarity).


==About this Structure==
==About this Structure==
[[3ner]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NER OCA].  
[[3ner]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NER OCA].  


==See Also==
==Reference==
*[[Cytochrome b5|Cytochrome b5]]
<ref group="xtra">PMID:021574570</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Benson, D B.]]
[[Category: Benson, D B.]]

Revision as of 08:31, 19 June 2013

Template:STRUCTURE 3ner

Structure of Human Type B Cytochrome b5

Template:ABSTRACT PUBMED 21574570

Function

[CYB5B_HUMAN] Cytochrome b5 is a membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases (By similarity).

About this Structure

3ner is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  1. 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

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