Any feedback?
Literature summary for 4.2.99.B1 extracted from
- Backbone dynamics and refined solution structure of the N-terminal domain of DNA polymerase beta. Correlation with DNA binding and dRP lyase activity (2000), J. Mol. Biol., 296, 229-253.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| the active-site pocket of dRP lyase is formed by the residues K72, Y39, and K35. K72 directly participates in Schiff base formation on the ring-opened form of the 5'-dRP group bound at the active-site pocket. Backbone motion at the active-site residues is restricted | Rattus norvegicus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| dRP lyase | - |
Rattus norvegicus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
