Literature summary for 1.6.2.4 extracted from

Hussain, R.; Ahmed, M.; Khan, T.A.; Akhter, Y.
Augmentation of cytochrome P450 monooxygenase catalysis on its interaction with NADPH-cytochrome P450 reductase FMN domain from Trichoderma brevicompactum (2018), Int. J. Biochem. Cell Biol., 103, 74-80 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling of a complex of the FMN domain with cytochrome P450 monooxygenase Tri11. The complex shows significant interface contacts and structural changes on interaction, the hydrogen bonding interactions are observed between Tri11 protein residues R91, R97, K127, P131,K136, Q139, E275, K375, R411, W412, E415, A416, K417, T418, N419, S421, S422, P423, W424, Y425, N426, D427, R428, R429, N436, V437, G438, R440, N441, R445 and CPR FMN domain residues D132, E102, E78, Y70, S82, R83, E202, E208, T96, N169, Y172, T171, G203, A204, T74, Q73, Y125, E127, E173, G128, E129, T131, S177, T76, A77, G75, A123, D100, N133, S72	Trichoderma brevicompactum

Crystallization (Comment)

Organism

modeling of a complex of the FMN domain with cytochrome P450 monooxygenase Tri11. The complex shows significant interface contacts and structural changes on interaction, the hydrogen bonding interactions are observed between Tri11 protein residues R91, R97, K127, P131,K136, Q139, E275, K375, R411, W412, E415, A416, K417, T418, N419, S421, S422, P423, W424, Y425, N426, D427, R428, R429, N436, V437, G438, R440, N441, R445 and CPR FMN domain residues D132, E102, E78, Y70, S82, R83, E202, E208, T96, N169, Y172, T171, G203, A204, T74, Q73, Y125, E127, E173, G128, E129, T131, S177, T76, A77, G75, A123, D100, N133, S72

Trichoderma brevicompactum

Organism

Organism	UniProt	Comment	Textmining
Trichoderma brevicompactum	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)