2R1R
RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI
Summary for 2R1R
Entry DOI | 10.2210/pdb2r1r/pdb |
Descriptor | RIBONUCLEOTIDE REDUCTASE R1 PROTEIN, RIBONUCLEOTIDE REDUCTASE R2 PROTEIN, THYMIDINE-5'-TRIPHOSPHATE (3 entities in total) |
Functional Keywords | ribonucleotide reductase, deoxyribonucleotide synthesis, radical chemistry, allosteric regulation, specificity, complex (oxidoreductase-peptide), complex (oxidoreductase-peptide) complex, complex (oxidoreductase/peptide) |
Biological source | Escherichia coli More |
Total number of polymer chains | 7 |
Total formula weight | 268163.33 |
Authors | Eriksson, M.,Eklund, H. (deposition date: 1997-07-21, release date: 1998-01-28, Last modification date: 2011-07-13) |
Primary citation | Eriksson, M.,Uhlin, U.,Ramaswamy, S.,Ekberg, M.,Regnstrom, K.,Sjoberg, B.M.,Eklund, H. Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure, 5:1077-1092, 1997 Cited by PubMed: 9309223DOI: 10.1016/S0969-2126(97)00259-1 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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