From Wikipedia, the free encyclopedia
![](http://upload.wikimedia.org/wikipedia/commons/thumb/2/29/3chy_flavodoxin_fold.png/300px-3chy_flavodoxin_fold.png)
The flavodoxin fold is a common α/β protein fold, second only to the TIM barrel fold. It has three layers, with two α-helical layers sandwiching a 5-stranded parallel β-sheet. The order of strands within the sheet is 2-1-3-4-5.
This motif is present for example in lactate dehydrogenase (PDB: 1A5Z) or phosphoglycerate kinase (PDB: 1FW8).[1]
External links
[edit]- SCOP list of proteins adopting the flavodoxin fold Archived 2018-12-07 at the Wayback Machine (mirror)
References
[edit]- ^ Kalinowska B, Banach M, Wiśniowski Z, Konieczny L, Roterman I (July 2017). "Is the hydrophobic core a universal structural element in proteins?". Journal of Molecular Modeling. 23 (7): 205. doi:10.1007/s00894-017-3367-z. PMC 5487895. PMID 28623601.
General | |
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All-α folds: | |
All-β folds: | |
α/β folds: | |
α+β folds: | |
Irregular folds: |
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