Cloned (Comment) | Organism |
---|---|
expression of His-tagged wild-type and mutant enzymes in Escherichia coli | Comamonas testosteroni |
Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of insertion mutants, overview | Comamonas testosteroni |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Comamonas testosteroni | P80702 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography | Comamonas testosteroni |
Subunits | Comment | Organism |
---|---|---|
dimer | the dimerization takes place via an interface axis. The formation of a tetramer is blocked in 3alpha-HSD/CR by the presence of a predominantly alpha-helical subdomain which is missing in all other SDRs of known structure, overview | Comamonas testosteroni |
More | domain structure, the enzyme possessses a 28 amino acids insertion into the classical Rossmann-fold motif between strand betaE and helix alphaF, preventing the formation of a four helix bundle and enables the dimerization via a P-axis interface, structure homology modelling and simulation, structure comparison, overview | Comamonas testosteroni |
Synonyms | Comment | Organism |
---|---|---|
3alpha-HSD/CR | - |
Comamonas testosteroni |
More | cf. EC 1.1.1.213, the enzyme belongs to the short chain dehydrogenase/reductase protein superfamily | Comamonas testosteroni |