Literature summary for 1.13.11.55 extracted from

Li, M.; Chen, Z.; Zhang, P.; Pan, X.; Jiang, C.; An, X.; Liu, S.; Chang, W.
Crystal structure studies on sulfur oxygenase reductase from Acidianus tengchongensis (2008), Biochem. Biophys. Res. Commun., 369, 919-923.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion technique	Acidianus tengchongensis

Protein Variants

Protein Variants	Comment	Organism
C101S	mutation of any cysteine residues (C31S, C101S, and C104S) at the active site leads to complete loss of SOR catalytic ability	Acidianus tengchongensis
C104S	mutation of any cysteine residues (C31S, C101S, and C104S) at the active site leads to complete loss of SOR catalytic ability	Acidianus tengchongensis
C31S	mutation of any cysteine residues (C31S, C101S, and C104S) at the active site leads to complete loss of SOR catalytic ability	Acidianus tengchongensis
His86F	mutation results in a dramatic reduction in SOR activity	Acidianus tengchongensis
His90F	mutation results in a dramatic reduction in SOR activity	Acidianus tengchongensis

Organism

Organism	UniProt	Comment	Textmining
Acidianus tengchongensis	-	-	-

Subunits

Subunits	Comment	Organism
More	24 identical SOR monomers form a hollow sphere. Within the icosatetramer sphere, the tetramer and trimer channels are proposed as the paths for the substrate and products, respectively	Acidianus tengchongensis

Synonyms

Synonyms	Comment	Organism
SOR-AT	-	Acidianus tengchongensis
sulfur oxygenase reductase	-	Acidianus tengchongensis

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Release 2023.1 (January 2023)