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PDB: 4 results

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BU of 4r1r by Molmil

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI
Descriptor:	GUANOSINE-5'-DIPHOSPHATE, RIBONUCLEOTIDE REDUCTASE R1 PROTEIN, RIBONUCLEOTIDE REDUCTASE R2 PROTEIN, ...
Authors:	Eriksson, M, Eklund, H.
Deposit date:	1997-07-22
Release date:	1998-01-28
Last modified:	2024-02-28
Method:	X-RAY DIFFRACTION (3.2 Å)
Cite:	Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure, 5, 1997

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BU of 3r1r by Molmil

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI
Descriptor:	ADENOSINE-5'-TRIPHOSPHATE, RIBONUCLEOTIDE REDUCTASE R1 PROTEIN, RIBONUCLEOTIDE REDUCTASE R2 PROTEIN
Authors:	Eriksson, M, Eklund, H.
Deposit date:	1997-07-21
Release date:	1998-01-28
Last modified:	2011-07-13
Method:	X-RAY DIFFRACTION (3 Å)
Cite:	Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure, 5, 1997

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BU of 2r1r by Molmil

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI
Descriptor:	RIBONUCLEOTIDE REDUCTASE R1 PROTEIN, RIBONUCLEOTIDE REDUCTASE R2 PROTEIN, THYMIDINE-5'-TRIPHOSPHATE
Authors:	Eriksson, M, Eklund, H.
Deposit date:	1997-07-21
Release date:	1998-01-28
Last modified:	2011-07-13
Method:	X-RAY DIFFRACTION (3 Å)
Cite:	Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure, 5, 1997

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BU of 1r1r by Molmil

RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI
Descriptor:	RIBONUCLEOTIDE REDUCTASE R1 PROTEIN, RIBONUCLEOTIDE REDUCTASE R2 PROTEIN
Authors:	Eriksson, M, Eklund, H.
Deposit date:	1997-07-15
Release date:	1998-01-28
Last modified:	2024-02-14
Method:	X-RAY DIFFRACTION (2.9 Å)
Cite:	Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding. Structure, 5, 1997

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