2l8m
From Proteopedia
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[[Image:2l8m.png|left|200px]] | [[Image:2l8m.png|left|200px]] | ||
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{{STRUCTURE_2l8m| PDB=2l8m | SCENE= }} | {{STRUCTURE_2l8m| PDB=2l8m | SCENE= }} | ||
===Reduced and CO-bound cytochrome P450cam (CYP101A1)=== | ===Reduced and CO-bound cytochrome P450cam (CYP101A1)=== | ||
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{{ABSTRACT_PUBMED_21265500}} | {{ABSTRACT_PUBMED_21265500}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2l8m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8M OCA]. | + | [[2l8m]] is a 1 chain structure of [[Cytochrome P450]] with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L8M OCA]. |
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| + | ==See Also== | ||
| + | *[[Cytochrome P450|Cytochrome P450]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:021265500</ref><references group="xtra"/> |
[[Category: Camphor 5-monooxygenase]] | [[Category: Camphor 5-monooxygenase]] | ||
[[Category: Pseudomonas putida]] | [[Category: Pseudomonas putida]] | ||
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[[Category: Pochapsky, S S.]] | [[Category: Pochapsky, S S.]] | ||
[[Category: Pochapsky, T C.]] | [[Category: Pochapsky, T C.]] | ||
| + | [[Category: Metalloenzyme]] | ||
| + | [[Category: Monooxygenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 02:56, 26 July 2012
Contents |
Reduced and CO-bound cytochrome P450cam (CYP101A1)
Template:ABSTRACT PUBMED 21265500
About this Structure
2l8m is a 1 chain structure of Cytochrome P450 with sequence from Pseudomonas putida. Full experimental information is available from OCA.
See Also
Reference
- Asciutto EK, Dang M, Pochapsky SS, Madura JD, Pochapsky TC. Experimentally Restrained Molecular Dynamics Simulations for Characterizing the Open States of Cytochrome P450(cam). Biochemistry. 2011 Feb 8. PMID:21265500 doi:10.1021/bi101820d
