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Literature summary 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.
    View publication on PubMed

Crystallization (Commentary)

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

Protein Variants

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

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.55 Acidianus tengchongensis
-
-
-

Subunits

EC Number Subunits Comment Organism
1.13.11.55 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

EC Number Synonyms Comment Organism
1.13.11.55 SOR-AT
-
 Acidianus tengchongensis
1.13.11.55 sulfur oxygenase reductase
-
 Acidianus tengchongensis