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Structure of cytochrome P450 2B4 with an acetate ligand and an active site hydrogen bond network similar to oxyferrous P450cam
Superposition of the active site of acetate-bound P4502B4 and oxyferrous P450cam. Bond lengths between the heme iron, the sixth ligand, and the hydroxyl of the conserved threonine are shown. Note that different threonine rotamers form the hydrogen bonds to the acetate and oxygen. [Image: see text]
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| Udgivet i: | J Inorg Biochem |
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| Main Authors: | , , , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
2018
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5995674/ https://ncbi.nlm.nih.gov/pubmed/29730233 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jinorgbio.2018.04.015 |
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