Literature summary for 1.6.2.2 extracted from

Benson, D.; Lovell, S.; Mehzabeen, N.; Galeva, N.; Cooper, A.; Gao, P.; Battaile, K.; Zhu, H.
Crystal structures of the naturally fused CS and cytochrome b5 reductase (b5R) domains of Ncb5or reveal an expanded CS fold, extensive CS-b5R interactions and productive binding of the NAD(P)+ nicotinamide ring (2019), Acta Crystallogr. Sect. D, 75, 628-638 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of a construct comprising the naturally fused CHORD-Sgt1 and b5R domains with bound FAD and NAD+ or NADP+. The linker between the CHORD-Sgt1 and b5R cores is more ordered than predicted, with much of it extending the beta-sandwich motif of the CHORD-Sgt1 domain. This limits the flexibility between the two domains	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q7L1T6	-	-

Synonyms

Synonyms	Comment	Organism
Cyb5R4	-	Homo sapiens
Ncb5or	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	NAD+ and NADP+ bind with the nicotinamide ring in the active site	Homo sapiens
NADP+	NAD+ and NADP+ bind with the nicotinamide ring in the active site	Homo sapiens

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Release 2023.1 (January 2023)