3R1R

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI

Summary for 3R1R

• Entry DOI: 10.2210/pdb3r1r/pdb
• Descriptor: RIBONUCLEOTIDE REDUCTASE R1 PROTEIN, RIBONUCLEOTIDE REDUCTASE R2 PROTEIN, ADENOSINE-5'-TRIPHOSPHATE, ... (4 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
• Total number of polymer chains: 7
• Total formula weight: 268238.37

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; PubMed: 9309223; DOI: 10.1016/S0969-2126(97)00259-1

Experimental method

X-RAY DIFFRACTION (3 Å)