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Literature summary for 3.6.1.13 extracted from
- Structure of an N-terminally truncated Nudix hydrolase DR2204 from Deinococcus radiodurans (2009), Acta Crystallogr. Sect. F, 65, 1083-1087.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Deinococcus radiodurans |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| gadolinium derivative, to 2.0 A resolution. The crystal structure of DR2204 consists of the conserved alpha/beta/alpha sandwich fold typical of Nudix hydrolases, the Nudix box, residues 94-115, holding the alpha1 helix sits between two loops accessible to the solvent, while the other two helices, alpha2 and alpha3, lie on the other side of the central beta-sheet and participate in dimer-interface formation | Deinococcus radiodurans |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 21800 | - |
2 * 21800, calculated and gel filtration | Deinococcus radiodurans |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Deinococcus radiodurans | Q9RSC1 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme | Deinococcus radiodurans |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | 2 * 21800, calculated and gel filtration | Deinococcus radiodurans |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DR2204 | - |
Deinococcus radiodurans |
| Nudix hydrolase | - |
Deinococcus radiodurans |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Deinococcus radiodurans | calculated | - |
4.9 |
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Release 2023.1 (January 2023)
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