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Literature summary for 3.4.22.69 extracted from

  • Xu, T.; Ooi, A.; Lee, H.C.; Wilmouth, R.; Liu, D.X.; Lescar, J.
    Structure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer (2005), Acta Crystallogr. Sect. F, 61, 964-966.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
fused to maltose-binding protein and expressed in E. coli BL21 Severe acute respiratory syndrome-related coronavirus

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals grown in hanging-drop vapour-diffusion method Severe acute respiratory syndrome-related coronavirus

Organism

Organism UniProt Comment Textmining
Severe acute respiratory syndrome-related coronavirus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
fused to maltose-binding protein, removing the maltose-binding protein by cleavage with factor Xa, purification by Phenyl Sepharose column chromatography Severe acute respiratory syndrome-related coronavirus

Subunits

Subunits Comment Organism
dimer one monomer per asymmetric unit, dimer is generated through the crystallographic twofold Severe acute respiratory syndrome-related coronavirus

Synonyms

Synonyms Comment Organism
SARS CoV main proteinase
-
Severe acute respiratory syndrome-related coronavirus