Literature summary for 1.13.11.66 extracted from

Machonkin, T.E.; Holland, P.L.; Smith, K.N.; Liberman, J.S.; Dinescu, A.; Cundari, T.R.; Rocks, S.S.
Determination of the active site of Sphingobium chlorophenolicum 2,6-dichlorohydroquinone dioxygenase (PcpA) (2010), J. Biol. Inorg. Chem., 15, 291-301.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Sphingobium chlorophenolicum

Crystallization (Commentary)

Crystallization (Comment)	Organism
generation of a homology model, based on zinc protein PDB entry 1ZSW, which predicts that the tertiary structure of the enzyme differs significantly from that of the extradiol dioxygenases, and that the residues ligating the Fe(II) are H11, H227, and E276	Sphingobium chlorophenolicum

Protein Variants

Protein Variants	Comment	Organism
E276A	less than 6% of wild-type activity	Sphingobium chlorophenolicum
H11A	less than 6% of wild-type activity	Sphingobium chlorophenolicum
H159A	67% of wild-type activity	Sphingobium chlorophenolicum
H227A	less than 6% of wild-type activity	Sphingobium chlorophenolicum
Y266F	about 6% of wild-type activity	Sphingobium chlorophenolicum

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	the residues ligating the Fe(II) are H11, H227, and E276	Sphingobium chlorophenolicum

Organism

Organism	UniProt	Comment	Textmining
Sphingobium chlorophenolicum	Q9ZBB0	-	-

Synonyms

Synonyms	Comment	Organism
PcpA	-	Sphingobium chlorophenolicum

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Release 2023.1 (January 2023)