Literature summary for 7.2.1.1 extracted from

Borshchevskiy, V.; Round, E.; Bertsova, Y.; Polovinkin, V.; Gushchin, I.; Ishchenko, A.; Kovalev, K.; Mishin, A.; Kachalova, G.; Popov, A.; Bogachev, A.; Gordeliy, V.
Structural and functional investigation of flavin binding center of the NqrC subunit of sodium-translocating NADH: Quinone oxidoreductase from Vibrio harveyi (2015), PLoS ONE, 10, e0118548.

Crystallization (Commentary)

Crystallization (Comment)	Organism
holo-enzyme, to 1.56 A resolution. The isoalloxazine moiety of the FMN residue is buried in a hydrophobic cavity and its pyrimidine ring is squeezed between hydrophobic amino acid residues while its benzene ring is extended from the protein surroundings. This structure of the flavin-binding pocket appears to provide flexibility of the benzene ring, which can help the FMN residue to take the bended conformation and to stabilize the one-electron reduced form of the prosthetic group, and may also lead to relatively weak noncovalent binding of the flavin	Vibrio harveyi

Crystallization (Comment)

Organism

holo-enzyme, to 1.56 A resolution. The isoalloxazine moiety of the FMN residue is buried in a hydrophobic cavity and its pyrimidine ring is squeezed between hydrophobic amino acid residues while its benzene ring is extended from the protein surroundings. This structure of the flavin-binding pocket appears to provide flexibility of the benzene ring, which can help the FMN residue to take the bended conformation and to stabilize the one-electron reduced form of the prosthetic group, and may also lead to relatively weak noncovalent binding of the flavin

Vibrio harveyi

Organism

Organism	UniProt	Comment	Textmining
Vibrio harveyi	-	subunit NqrC	-
Vibrio harveyi CAIM 1792	-	subunit NqrC	-

Cofactor

Cofactor	Comment	Organism	Structure
FMN	the isoalloxazine moiety of the FMN residue is buried in a hydrophobic cavity and its pyrimidine ring is squeezed between hydrophobic amino acid residues while its benzene ring is extended from the protein surroundings. This structure of the flavin-binding pocket appears to provide flexibility of the benzene ring, which can help the FMN residue to take the bended conformation and to stabilize the one-electron reduced form of the prosthetic group, and may also lead to relatively weak noncovalent binding of the flavin	Vibrio harveyi

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Release 2023.1 (January 2023)