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Literature summary for 1.17.4.1 extracted from
- Structure and function of the Escherichia coli ribonucleotide reductase protein R2 (1993), J. Mol. Biol., 232, 123-164.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| free radical subunit R2, basic motif is a bundle of eight long helices. R2 dimer has two equivalent dinuclear iron centers. Iron atoms have both histidine and carboxyl acid ligands and are bridged by the carboxylate group of E115. The essential residue Y122 is buried inside the protein and the tyrosyl radical cannot participate directly in hydrogen abstraction | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | subunit R2 dimer has two equivalent dinuclear iron centers. Iron atoms have both histidine and carboxyl acid ligands and are bridged by the carboxylate group of E115 | Escherichia coli |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
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