Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Cofactor

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search
Image of 2D Structure
Search for synonyms (with exact matching search term)

Search term:

Results 1 - 4 of 4
download as CSV
download all results as CSV
EC Number Cofactor Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B52NADH - 728893, 729146, 729854, 741676
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B52NADH no activity with NADPH, 3-quinuclidinone reductase BacC 729032
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B52NADH no activity with NADPH, 3-quinuclidinone reductase QNR 729032
Display the word mapDisplay the reaction diagram Show all sequences 1.1.1.B52NADH three NADH-bound protomers and one NADH-free protomer form a tetrameric structure in an asymmetric unit of crystals. NADH not only acts as a proton donor, but also contributes to the stability of the alpha7 helix. NADH is located in a deep cleft of the large domain and bound at the C-terminal end of the beta-sheet. The adenosine moiety of NADH is bound to a pocket formed by Gly16, Leu41, Val62, Asp63, Val64, Thr65, Ala91, Val93, and Val113. Residue Asp40 plays an important role in binding to NADH 741816
Results 1 - 4 of 4
download as CSV
download all results as CSV