Literature summary for 1.3.3.16 extracted from

Bent, A.F.; Mann, G.; Houssen, W.E.; Mykhaylyk, V.; Duman, R.; Thomas, L.; Jaspars, M.; Wagner, A.; Naismith, J.H.
Structure of the cyanobactin oxidase ThcOx fromCyanothece sp. PCC 7425, the first structure to be solved at Diamond Light Source beamline I23 by means of S-SAD (2016), Acta Crystallogr. Sect. D, 72, 1174-1180 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 3.15 A resolution, space group P412121 with two molecules found in the asymmetric unit. The structure is composed of a novel domain and an FMN nitroreductase domain. The N-terminal domain contains a portion (residues 7-86) which possesses the same fold as the leader binding domain of TruD, the so-called peptide-clamp domain. The C-terminal domain (residues 323-469) contains the FMN molecule and has a high degree of homology to the putative nitroreductase from Anabaena variabilis	Cyanothece sp. PCC 7425

Crystallization (Comment)

Organism

to 3.15 A resolution, space group P412121 with two molecules found in the asymmetric unit. The structure is composed of a novel domain and an FMN nitroreductase domain. The N-terminal domain contains a portion (residues 7-86) which possesses the same fold as the leader binding domain of TruD, the so-called peptide-clamp domain. The C-terminal domain (residues 323-469) contains the FMN molecule and has a high degree of homology to the putative nitroreductase from Anabaena variabilis

Cyanothece sp. PCC 7425

Organism

Organism	UniProt	Comment	Textmining
Cyanothece sp. PCC 7425	B8HTZ1	-	-

Synonyms

Synonyms	Comment	Organism
Cyan7425_0520	-	Cyanothece sp. PCC 7425
ThcOx	-	Cyanothece sp. PCC 7425

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Release 2023.1 (January 2023)