Literature summary extracted from

Huang, Y.; Duan, Y.; Zhang, Y.; Fan, P.; Li, Z.; Liu, W.; Cui, Z.
Crystal structure of hydroxyquinol 1,2-dioxygenase PnpC from Pseudomonas putida DLL-E4 and its role of N-terminal domain for catalysis (2018), Biochem. Biophys. Res. Commun., 507, 267-273 .

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.13.11.37	structure at 2.1 A resolution. The catalytic Fe(III) is pentacoordinated by the conserved Tyr160, Tyr194, His218 and His220 residues, the citrate anion and one water molecule. Asp80, Thr81 and Val248 are responsible for the substrate specificity. The N-terminal domain is required for its soluble expression and enzyme catalysis	Pseudomonas putida

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.13.11.37	Pseudomonas putida	C6FI44	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.13.11.37	PnpC	-	Pseudomonas putida

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Release 2023.1 (January 2023)