Literature summary extracted from

Chen, Q.; Huang, Y.; Duan, Y.; Li, Z.; Cui, Z.; Liu, W.
Crystal structure of p-nitrophenol 4-monooxygenase PnpA from Pseudomonas putida DLL-E4 The key enzyme involved in p-nitrophenol degradation (2018), Biochem. Biophys. Res. Commun., 504, 715-720 .

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.14.13.167	structure in its apo and FAD-complex to a resolution of 2.04 A and 2.48 A, respectively. The 4-nitrophenol substrate lies near the N5 edge of isoalloxazine ring in the protein interior. The bound substrate is rotated 60° with respect to pOHB deviating from the isoalloxazine. The nitro group of 4-nitrophenol is directly hydrogen bonded to Val54 and Arg234, and the hydroxyl group is hydrogen bonded to Val223 and Cys23	Pseudomonas putida

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.14.13.167	Pseudomonas putida	C6FI48	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.14.13.167	pnpA	-	Pseudomonas putida

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.14.13.167	FAD	the open position of the isoalloxazine ring is anchored by directed or water-mediated hydrogen bonds to the side chains of Ser311 and Arg234. The ribityl moiety of FAD forms hydrogen bonds to Arg52 and Gln115. The phosphate moiety of FAD interacts with the conserved GXGXXG motif and GD motif. The ribose moiety of ADP is held by the hydrogen bonds to Glu42, Ser43 and Glu44. The adenine ring of FAD interacts with Val140 and Thr177	Pseudomonas putida

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Release 2023.1 (January 2023)