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3ejd
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 3EJD is a | + | 3EJD is a 8 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EJD OCA]. |
==Reference== | ==Reference== | ||
| - | + | <ref group="xtra">PMID:18838690</ref><references group="xtra"/> | |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Cryle, M J.]] | [[Category: Cryle, M J.]] | ||
[[Category: Schlichting, I.]] | [[Category: Schlichting, I.]] | ||
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[[Category: Protein-protein complex]] | [[Category: Protein-protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:10:50 2009'' |
Revision as of 14:10, 16 February 2009
Crystal Structure of P450BioI in complex with hexadec-9Z-enoic acid ligated Acyl Carrier Protein
Template:ABSTRACT PUBMED 18838690
About this Structure
3EJD is a 8 chains structure of sequences from Bacillus subtilis and Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Cryle MJ, Schlichting I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex. Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15696-701. Epub 2008 Oct 6. PMID:18838690
Page seeded by OCA on Mon Feb 16 16:10:50 2009
Categories: Bacillus subtilis | Escherichia coli | Cryle, M J. | Schlichting, I. | 4-helix bundle | Biotin biosynthesis | Carrier protein | Cytochrome p450 fold | Cytoplasm | Fatty acid biosynthesis | Heme | Iron | Lipid synthesis | Metal-binding | Monooxygenase | Oxidoreductase | Oxidoreductase/lipid transport complex | Phosphopantetheine | Protein-protein complex
