1RLR
STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1
Summary for 1RLR
| Entry DOI | 10.2210/pdb1rlr/pdb |
| Descriptor | RIBONUCLEOTIDE REDUCTASE PROTEIN R1 (1 entity in total) |
| Functional Keywords | reductase (acting on ch2), oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 86010.27 |
| Authors | Uhlin, U.,Eklund, H. (deposition date: 1994-08-12, release date: 1996-12-23, Last modification date: 2024-11-20) |
| Primary citation | Uhlin, U.,Eklund, H. Structure of ribonucleotide reductase protein R1. Nature, 370:533-539, 1994 Cited by PubMed Abstract: Ribonucleotide reductase is the only enzyme that catalyses de novo formation of deoxyribonucleotides and is thus a key enzyme in DNA synthesis. The radical-based reaction involves five cysteins. Two redox-active cysteines are located at adjacent antiparallel strands in a new type of ten-stranded alpha/beta-barrel, and two others at the carboxyl end in a flexible arm. The fifth cysteine, in a loop in the centre of the barrel, is positioned to initiate the radical reaction. PubMed: 8052308DOI: 10.1038/370533a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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