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1qfn

GLUTAREDOXIN-1-RIBONUCLEOTIDE REDUCTASE B1 MIXED DISULFIDE BOND

Method: SOLUTION NMR Dmax: 41.3 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PROTEIN (GLUTAREDOXIN 1)

Escherichia coli

UniProt P68688

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–85 Mutation：C14S PROTEIN (RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1) × 1 （P00452） SOLUTION NMR NMR measurement conditions：pH 6.5；293 K；Pressure 1 Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1QFN Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1EGO NMR STRUCTURE OF OXIDIZED ESCHERICHIA COLI GLUTAREDOXIN: COMPARISON WITH REDUCED E. COLI GLUTAREDOXIN AND FUNCTIONALLY RELATED PROTEINS Deposited 1991-10-08 Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–85（85 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1EGR SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN Deposited 1991-10-08 Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–85（85 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1GRX STRUCTURE OF E. COLI GLUTAREDOXIN Deposited 1993-10-01 Different oligomeric state Different ligand/ion Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–85（85 aa）
Mutation：C14S GSH Glutathione × 1 SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLRX1_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–85； UniProt 1–85

PROTEIN (RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1)

Escherichia coli

UniProt P00452

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 737–761 Fragment：apha chain, B1 SUBUNIT Mutation：C754S PROTEIN (GLUTAREDOXIN 1) × 1 （P68688） SOLUTION NMR NMR measurement conditions：pH 6.5；293 K；Pressure 1 Resolution not provided

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 1QFN Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–761（761 aa）
Mutation：Y730F No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 2.90 Å R-free 0.245
1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–761（761 aa）
Mutation：Y730F No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 2.90 Å R-free 0.245
1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–761（761 aa）
Mutation：Y730F No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 2.90 Å R-free 0.245
1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：Y730F Mutation：Y730F No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 2.90 Å R-free 0.245
1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa）
Mutation：Y730F No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 2.90 Å R-free 0.245
1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：Y730F Mutation：Y730F No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 2.90 Å R-free 0.245
1RLR STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1 Deposited 1994-08-12 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–761（761 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.280
2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.280
2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.280
2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.280
2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.280
2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.280
2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.280
2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.280
2X0X Ribonucleotide reductase R1 subunit of E. coli to 2.3 A resolution Deposited 2009-12-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa）
Not recorded SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE APP 1.5M, SODIUM CITRATE BUFFER PH APP 6.
Resolution 2.30 Å R-free 0.224
2X0X Ribonucleotide reductase R1 subunit of E. coli to 2.3 A resolution Deposited 2009-12-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded SO4 SULFATE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE APP 1.5M, SODIUM CITRATE BUFFER PH APP 6.
Resolution 2.30 Å R-free 0.224
2XAK Ribonucleotide reductase Y730NO2Y modified R1 subunit of E. coli Deposited 2010-03-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：RESIDUES 1-761
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.80 Å R-free 0.241
2XAK Ribonucleotide reductase Y730NO2Y modified R1 subunit of E. coli Deposited 2010-03-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：RESIDUES 1-761
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.80 Å R-free 0.241
2XAP Ribonucleotide reductase Y731NO2Y modified R1 subunit of E. coli to 2. 1 A resolution Deposited 2010-03-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：RESIDUES 1-761
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.10 Å R-free 0.230
2XAP Ribonucleotide reductase Y731NO2Y modified R1 subunit of E. coli to 2. 1 A resolution Deposited 2010-03-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：RESIDUES 1-761
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.10 Å R-free 0.230
2XAV Ribonucleotide reductase Y731NO2Y and Y730F modified R1 subunit of E. coli Deposited 2010-03-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.80 Å R-free 0.247
2XAV Ribonucleotide reductase Y731NO2Y and Y730F modified R1 subunit of E. coli Deposited 2010-03-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.80 Å R-free 0.247
2XAW Ribonucleotide reductase Y730NO2Y and Y731F modified R1 subunit of E. coli Deposited 2010-03-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 3.10 Å R-free 0.234
2XAW Ribonucleotide reductase Y730NO2Y and Y731F modified R1 subunit of E. coli Deposited 2010-03-31 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 3.10 Å R-free 0.234
2XAX Ribonucleotide reductase Y730NO2Y and Y731A modified R1 subunit of E. coli Deposited 2010-04-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.75 Å R-free 0.261
2XAX Ribonucleotide reductase Y730NO2Y and Y731A modified R1 subunit of E. coli Deposited 2010-04-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.75 Å R-free 0.261
2XAY Ribonucleotide reductase Y730NO2Y and C439A modified R1 subunit of E. coli Deposited 2010-04-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.65 Å R-free 0.235
2XAY Ribonucleotide reductase Y730NO2Y and C439A modified R1 subunit of E. coli Deposited 2010-04-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.65 Å R-free 0.235
2XAZ Ribonucleotide reductase Y730NO2Y and C439S modified R1 subunit of E. coli Deposited 2010-04-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.60 Å R-free 0.246
2XAZ Ribonucleotide reductase Y730NO2Y and C439S modified R1 subunit of E. coli Deposited 2010-04-01 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：RESIDUES 1-761
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.60 Å R-free 0.246
2XO4 RIBONUCLEOTIDE REDUCTASE Y730NH2Y MODIFIED R1 SUBUNIT OF E. COLI Deposited 2010-08-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：RESIDUES 1-761
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.50 Å R-free 0.233
2XO4 RIBONUCLEOTIDE REDUCTASE Y730NH2Y MODIFIED R1 SUBUNIT OF E. COLI Deposited 2010-08-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：RESIDUES 1-761
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.50 Å R-free 0.233
2XO5 RIBONUCLEOTIDE REDUCTASE Y731NH2Y MODIFIED R1 SUBUNIT OF E. COLI Deposited 2010-08-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa） Fragment：CATALYTIC SUBUNIT, RESIDUES 1-761
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.70 Å R-free 0.228
2XO5 RIBONUCLEOTIDE REDUCTASE Y731NH2Y MODIFIED R1 SUBUNIT OF E. COLI Deposited 2010-08-09 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa） Fragment：CATALYTIC SUBUNIT, RESIDUES 1-761
Chain B 1–761（761 aa） Fragment：CATALYTIC SUBUNIT, RESIDUES 1-761
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
Resolution 2.70 Å R-free 0.228
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 8 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 9 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
Resolution 3.00 Å R-free 0.287
3UUS Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex Deposited 2011-11-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Chain C 1–761（761 aa）
Chain D 1–761（761 aa）
Not recorded DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 8 FE FE (III) ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；10.8% PEG 3350, 0.18M magnesium acetate, 0.09M MOPS pH 7.5, 0.01M iron (III) chloride, 4.5% glycerol , VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 5.65 Å R-free 0.303
4ERM Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex at 4 Angstroms resolution Deposited 2012-04-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Chain C 1–761（761 aa）
Chain D 1–761（761 aa）
Not recorded DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 8 DAT 2'-DEOXYADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 FEO MU-OXO-DIIRON × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Precipitant conditions: 10% PEG 3350, 0.1 M MOPS pH 7.5, 0.2 M Magnesium Acetate, 0.025 M Magnesium Chloride, 0.006 M n-Nonyl-beta-D-maltopyranoside, and 5% glycerol. Mixed 1:1 with protein., VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 3.95 Å R-free 0.284
4ERP Crystal structure of a gemcitabine-diphosphate inhibited E. coli class Ia ribonucleotide reductase complex Deposited 2012-04-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 4 FEO MU-OXO-DIIRON × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Precipitant solution: 25% PEG 3350, 0.1 M HEPES pH 7.5, 0.2 M ammonium acetate, 5% glycerol mixed 2:1 with protein and streak seeded from crystals grown under similar conditions. , VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 4.45 Å R-free 0.267
4ERP Crystal structure of a gemcitabine-diphosphate inhibited E. coli class Ia ribonucleotide reductase complex Deposited 2012-04-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain C 1–761（761 aa）
Chain D 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 4 FEO MU-OXO-DIIRON × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Precipitant solution: 25% PEG 3350, 0.1 M HEPES pH 7.5, 0.2 M ammonium acetate, 5% glycerol mixed 2:1 with protein and streak seeded from crystals grown under similar conditions. , VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 4.45 Å R-free 0.267
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–761（761 aa）
Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 10 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–761（761 aa）
Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–761（761 aa）
Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–761（761 aa）
Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：C292A Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa）
Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：C292A Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–761（761 aa）
Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：C292A Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 9 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：C292A Mutation：C292A TTP THYMIDINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
Resolution 3.20 Å R-free 0.308
5CNS Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to CDP and dATP at 2.97 Angstroms resolution Deposited 2015-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Chain C 1–761（761 aa）
Chain D 1–761（761 aa）
Not recorded CDP CYTIDINE-5'-DIPHOSPHATE × 4 DAT 2'-DEOXYADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 8 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 FEO MU-OXO-DIIRON × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；9.5% (w/v) PEG 3350, 100 mM MOPS, 250 mM Mg(CH3COO)2, 25 mM 394 MgCl2, 5% (v/v) glycerol
Resolution 2.98 Å R-free 0.214
5CNT Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to UDP and dATP at 3.25 Angstroms resolution Deposited 2015-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Chain C 1–761（761 aa）
Chain D 1–761（761 aa）
Not recorded UDP URIDINE-5'-DIPHOSPHATE × 4 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 8 FEO MU-OXO-DIIRON × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2% (w/v) PEG 3350, 100 mM MOPS pH 7.5, 300 mM Mg(CH3COO)2, 30 mM MgCl2, and 5% (v/v) glycerol
Resolution 3.25 Å R-free 0.221
5CNU Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to ADP and dGTP at 3.40 Angstroms resolution Deposited 2015-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Chain C 1–761（761 aa）
Chain D 1–761（761 aa）
Not recorded DGT 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 4 DAT 2'-DEOXYADENOSINE-5'-DIPHOSPHATE × 4 FEO MU-OXO-DIIRON × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2% (w/v) PEG 3350, 100 mM MOPS pH 7.5, 300 mM Mg(CH3COO)2, 30 mM MgCl2, and 5% (v/v) glycerol
Resolution 3.40 Å R-free 0.221
5CNV Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to GDP and TTP at 3.20 Angstroms resolution Deposited 2015-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Chain C 1–761（761 aa）
Chain D 1–761（761 aa）
Not recorded GDP GUANOSINE-5'-DIPHOSPHATE × 4 DAT 2'-DEOXYADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 8 TTP THYMIDINE-5'-TRIPHOSPHATE × 8 FEO MU-OXO-DIIRON × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2% (w/v) PEG 3350, 100 mM MOPS pH 7.5, 300 mM Mg(CH3COO)2, 30 mM MgCl2, and 5% (v/v) glycerol
Resolution 3.20 Å R-free 0.219
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 10 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441A Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 11 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 12 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441A Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain B 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 1–761（761 aa）
Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 9 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441A Mutation：E441A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.227
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–761（761 aa）
Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–761（761 aa）
Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–761（761 aa）
Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441D Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa）
Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441D Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441D Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–761（761 aa）
Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 9 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–761（761 aa）
Mutation：E441D No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.240
6W4X Holocomplex of E. coli class Ia ribonucleotide reductase with GDP and TTP Deposited 2020-03-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded TTP THYMIDINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 FEO MU-OXO-DIIRON × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；blot for 4.5 seconds before plunging
Resolution 3.60 Å
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 1–761（761 aa）
Mutation：E441Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.231
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–761（761 aa）
Mutation：E441Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.231
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 1–761（761 aa）
Mutation：E441Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.231
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 1–761（761 aa）
Mutation：E441Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.231
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441Q Mutation：E441Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.231
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441Q Mutation：E441Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.231
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain C 1–761（761 aa）
Mutation：E441Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.231
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Mutation：E441Q Mutation：E441Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
Resolution 3.10 Å R-free 0.231
8VHN Crystal Structure of E. coli class Ia ribonucleotide reductase alpha subunit bound to two ATP molecules Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 GOL GLYCEROL × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；8.0% (w/vol)PEG3350, 80 mM HEPES pH 7.3, 280 mM magnesium chloride, 4% (vol/vol) glycerol, 1.0% CYMAL-1 detergent
Resolution 2.62 Å R-free 0.209
8VHO Crystal Structure of E. coli class Ia ribonucleotide reductase alpha subunit bound to dATP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277.15 K；6.8% (w/vol) PEG3350, 80mM HEPES pH7.3, 280mM MgCl2, 4% (vol/vol) glycerol, and 1.0% CYMAL-1 detergent
Resolution 2.55 Å R-free 0.205
8VHP Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to CDP and two molecules of ATP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–760（760 aa）
Chain B 1–760（760 aa）
Mutation：W28A Mutation：W28A SO4 SULFATE ION × 12 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 CDP CYTIDINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；1.9 M ammonium sulfate, 4% (w/vol) PEG MME 500, 0.1 M bis-Tris pH 6.5
Resolution 2.61 Å R-free 0.209
8VHP Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to CDP and two molecules of ATP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–760（760 aa）
Chain D 1–760（760 aa）
Mutation：W28A Mutation：W28A SO4 SULFATE ION × 12 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 CDP CYTIDINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；1.9 M ammonium sulfate, 4% (w/vol) PEG MME 500, 0.1 M bis-Tris pH 6.5
Resolution 2.61 Å R-free 0.209
8VHP Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to CDP and two molecules of ATP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain E 1–760（760 aa）
Chain F 1–760（760 aa）
Mutation：W28A Mutation：W28A SO4 SULFATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 CDP CYTIDINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；1.9 M ammonium sulfate, 4% (w/vol) PEG MME 500, 0.1 M bis-Tris pH 6.5
Resolution 2.61 Å R-free 0.209
8VHP Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to CDP and two molecules of ATP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain G 1–760（760 aa）
Chain H 1–760（760 aa）
Mutation：W28A Mutation：W28A SO4 SULFATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 CDP CYTIDINE-5'-DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；1.9 M ammonium sulfate, 4% (w/vol) PEG MME 500, 0.1 M bis-Tris pH 6.5
Resolution 2.61 Å R-free 0.209
8VHQ Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and ATP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–760（760 aa）
Chain B 1–760（760 aa）
Mutation：W28A Mutation：W28A DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；6.5-7.0% (w/vol) PEG3350, 0.1M HEPES 7.0, 0.35M MgSO4, 5% (vol/vol) glycerol.
Resolution 3.40 Å R-free 0.233
8VHQ Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and ATP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–760（760 aa）
Chain D 1–760（760 aa）
Mutation：W28A Mutation：W28A DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；6.5-7.0% (w/vol) PEG3350, 0.1M HEPES 7.0, 0.35M MgSO4, 5% (vol/vol) glycerol.
Resolution 3.40 Å R-free 0.233
8VHR Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and GTP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–760（760 aa）
Chain B 1–760（760 aa）
Mutation：W28A Mutation：W28A DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；6.5-7.0% (w/vol) PEG3350, 0.1M HEPES 7.0, 0.35M MgSO4, 5% (vol/vol) glycerol
Resolution 3.55 Å R-free 0.243
8VHR Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and GTP Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 1–760（760 aa）
Chain D 1–760（760 aa）
Mutation：W28A Mutation：W28A DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；6.5-7.0% (w/vol) PEG3350, 0.1M HEPES 7.0, 0.35M MgSO4, 5% (vol/vol) glycerol
Resolution 3.55 Å R-free 0.243
8VHU Crystal structure of dATP bound E. coli class Ia ribonucleotide reductase alpha construct fused with the C-terminal tail of E. coli class Ia beta subunit Deposited 2024-01-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–734（734 aa）
Chain B 1–734（734 aa）
Mutation：Truncated final 8 residues of alpha,fused C-terminal 35 residues of beta Mutation：Truncated final 8 residues of alpha,fused C-terminal 35 residues of beta DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 NA SODIUM ION × 1 CL CHLORIDE ION × 6 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277.15 K；1.4M NaCl, 8% (w/vol) PEG 6000
Resolution 2.10 Å R-free 0.192
9DB2 Class Ia ribonucleotide reductase with mechanism-based inhibitor N3CDP Deposited 2024-08-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–761（761 aa）
Chain B 1–761（761 aa）
Not recorded DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 UNL UNKNOWN LIGAND × 1 A1A3L 4-amino-1-{(3xi)-3-C-amino-2-deoxy-5-O-[(S)-hydroxy(phosphonooxy)phosphoryl]-beta-D-threo-pentofuranosyl}pyrimidin-2(1H)-one × 1 FEO MU-OXO-DIIRON × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å

33 other PDB entries and 104 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RIR1_ECOLI
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–25； UniProt 737–761

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1qfn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1qfn
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1qfn
Deposition date deposition_date1999-04-12
Structure title titleGLUTAREDOXIN-1-RIBONUCLEOTIDE REDUCTASE B1 MIXED DISULFIDE BOND
Keywords keywordsGLUTAREDOXIN, RIBONUCLEOTIDE REDUCTASE, DISULFIDE, ELECTRON TRANSFER, ELECTRON TRANSPORT-OXIDOREDUCTASE COMPLEX; ELECTRON TRANSPORT/OXIDOREDUCTASE
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier15.58 Å
Radius of gyration Rg (electron density) rg_electron15.10 Å
Forward intensity I(0) i0910314000.00
Molecular weight molecular_weight243590.0 kDa
Excluded volume excluded_volume299540 ų
Envelope volume envelope_volume37815 ų
Hydration-shell volume shell_volume16745 ų
Envelope diameter envelope_diameter70.2 Å
Shell Rg shell_rg25.91 Å
Envelope Rg envelope_rg22.23 Å
Shape Rg shape_rg15.09 Å
Total Rg total_rg15.35 Å
Total atoms total_atoms33400
Residues n_residues2200
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax41.3 Å
Rg (real space) rg_real14.51 Å
Rg uncertainty (real space) rg_real_error0.07 Å
I(0) (real space) i0_real8.6460e+08
I(0) uncertainty (real space) i0_real_error7.5880e+06
Rg (reciprocal space) rg_reciprocal15.71 Å
I(0) (reciprocal space) i0_reciprocal910300000.0000
Solution quality estimate total_estimate0.6832
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary17.8 Å
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.337
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha3.5160
Highest regularization parameter α highest_alpha251300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.008; Oscil: 0.980; Stabil: 0.982; Sysdev: 0.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1qfna_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.1 — Thioltransferase

CATH v4.4 (1 domains)

Domain ID domain_id1qfnA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
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8. Citations (1)

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9. Files and Curves (10)