Literature summary for 1.13.11.37 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 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Organism	UniProt	Comment	Textmining
Pseudomonas putida	C6FI44	-	-

Synonyms

Synonyms	Comment	Organism
PnpC	-	Pseudomonas putida

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Release 2023.1 (January 2023)