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7ai8

Structure of Ribonucleotide reductase R2 from Escherichia coli collected by still serial crystallography on a COC membrane at a synchrotron source

Method: X-RAY DIFFRACTION Dmax: 71.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Ribonucleoside-diphosphate reductase 1 subunit beta

Escherichia coli (strain K12)

UniProt P69924

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–376 Not recorded FE FE (III) ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 7；294 K；34-37 % PAA 2100, 100 mM HEPES 7.0, 250-450 mM NaCl, 200 mM ammonium sulfate [and] 26% PAA 2100, 100 mM HEPES 7.0, 150 NaCl, 100 Malonate Resolution 2.10 Å R-free 0.219

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 7AI8 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1AV8 RIBONUCLEOTIDE REDUCTASE R2 SUBUNIT FROM E. COLI Deposited 1997-09-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–340（340 aa）
Chain B 1–340（340 aa）
Not recorded FEO MU-OXO-DIIRON × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.6；PROTEIN WAS CRYSTALLIZED FROM 80% SATURATED NACL, NEAR PHYSIOLOGICAL PH (PH 7.6)
Resolution 2.80 Å R-free 0.192
1BIQ RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN MUTANT E238A Deposited 1998-06-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa） Fragment：BETA CHAIN
Chain B 1–375（375 aa） Fragment：BETA CHAIN
Mutation：Y122F, E238A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：Y122F, E238A FE2 FE (II) ION × 3 FE FE (III) ION × 1 OH HYDROXIDE ION × 3 HG MERCURY (II) ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6；pH 6.0
Resolution 2.05 Å R-free 0.260
1JPR Mn substituted Ribonucleotide reductase R2 from E. coli oxidized by nitric oxide Deposited 2001-08-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Not recorded MN MANGANESE (II) ION × 4 HG MERCURY (II) ION × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；PEG 4000, sodium chloride, EMTS, MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.88 Å R-free 0.213
1JQC Mn substituted Ribonucleotide reductase R2 from E. Coli oxidized by hydrogen peroxide and hydroxylamine Deposited 2001-08-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Not recorded MN MANGANESE (II) ION × 4 HG MERCURY (II) ION × 13 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；peg 4000, MES, EMTS, sodium chloride, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.61 Å R-free 0.219
1MRR SUBSTITUTION OF MANGANESE FOR IRON IN RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI. SPECTROSCOPIC AND CRYSTALLOGRAPHIC CHARACTERIZATION Deposited 1992-07-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Not recorded MN MANGANESE (II) ION × 4 HG MERCURY (II) ION × 13 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1MXR High resolution structure of Ribonucleotide reductase R2 from E. coli in its oxidised (Met) form Deposited 2002-10-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Not recorded FE FE (III) ION × 4 HG MERCURY (II) ION × 11 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；PEG 4000, MES, NaCl, EMTS, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.42 Å R-free 0.185
1PFR RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN Deposited 1996-12-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–340（340 aa）
Chain B 1–340（340 aa）
Mutation：S211A Mutation：S211A FE FE (III) ION × 4 HG MERCURY (II) ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；HANGING DROP VAPOR DIFFUSION. CRYSTALLISED FROM 20% PEG 4000, 0.2M NACL, 0.1M MES PH 6.0, 1MM ETHYLMERCURY SALICYLATE., vapor diffusion - hanging drop
Resolution 2.20 Å
1PIM DITHIONITE REDUCED E. COLI RIBONUCLEOTIDE REDUCTASE R2 SUBUNIT, D84E MUTANT Deposited 2003-05-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Mutation：D84E Mutation：D84E FE FE (III) ION × 4 HG MERCURY (II) ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；310 K；20% PEG 4000, 200mM NaCl, 50mM MES, 0.3% dioxane, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Resolution 2.00 Å R-free 0.246
1PIU OXIDIZED RIBONUCLEOTIDE REDUCTASE R2-D84E MUTANT CONTAINING OXO-BRIDGED DIFERRIC CLUSTER Deposited 2003-05-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Mutation：D84E Mutation：D84E FE FE (III) ION × 4 HG MERCURY (II) ION × 10 O OXYGEN ATOM × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；310 K；20% PEG 4000, 200mM NaCl, 50mM MES, 0.3% dioxane, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Resolution 2.20 Å R-free 0.232
1PIY RIBONUCLEOTIDE REDUCTASE R2 SOAKED WITH FERROUS ION AT NEUTRAL PH Deposited 2003-05-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Not recorded FE FE (III) ION × 4 HG MERCURY (II) ION × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；310 K；20% PEG 4000, 200mM NaCl, 50mM MES, 0.3% dioxane, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Resolution 1.68 Å R-free 0.246
1PIZ RIBONUCLEOTIDE REDUCTASE R2 D84E MUTANT SOAKED WITH FERROUS IONS AT NEUTRAL PH Deposited 2003-05-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Mutation：D84E Mutation：D84E FE FE (III) ION × 4 HG MERCURY (II) ION × 11 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；310 K；20% PEG 4000, 200mM NaCl, 50mM MES, 0.3% dioxane, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Resolution 1.90 Å R-free 0.242
1PJ0 RIBONUCLEOTIDE REDUCTASE R2-D84E/W48F MUTANT SOAKED WITH FERROUS IONS AT NEUTRAL PH Deposited 2003-05-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Mutation：D84E, W48F Mutation：D84E, W48F FE FE (III) ION × 4 HG MERCURY (II) ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；310 K；20% PEG 4000, 200mM NaCl, 50mM MES, 0.3% dioxane, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Resolution 1.90 Å R-free 0.236
1PJ1 RIBONUCLEOTIDE REDUCTASE R2-D84E/W48F SOAKED WITH FERROUS IONS AT PH 5 Deposited 2003-05-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Mutation：D84E, W48F Mutation：D84E, W48F FE FE (III) ION × 4 HG MERCURY (II) ION × 15 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；310 K；20% PEG 4000, 200mM NaCl, 50mM MES, 0.3% dioxane, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Resolution 1.95 Å R-free 0.221
1PM2 CRYSTAL STRUCTURE OF MANGANESE SUBSTITUTED R2-D84E (D84E MUTANT OF THE R2 SUBUNIT OF E. COLI RIBONUCLEOTIDE REDUCTASE) Deposited 2003-06-09 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–339（339 aa）
Chain B 1–339（339 aa）
Mutation：D84E Mutation：D84E MN MANGANESE (II) ION × 4 HG MERCURY (II) ION × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.3；310 K；PEG 4000, MES, sodium chloride, sodium ethylmercurithiosalicylicate , pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Resolution 1.80 Å R-free 0.215
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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain P 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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
1R65 Crystal structure of ferrous soaked Ribonucleotide Reductase R2 subunit (wildtype) at pH 5 from E. coli Deposited 2003-10-14 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa） Fragment：Ribonucleotide Reductase R2
Chain B 1–375（375 aa） Fragment：Ribonucleotide Reductase R2
Not recorded FE2 FE (II) ION × 4 HG MERCURY (II) ION × 13 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；310 K；PEG4000, sodium chloride, EMTS, MES, pH 6, VAPOR DIFFUSION, HANGING DROP, temperature 310K
Resolution 1.95 Å R-free 0.236
1RIB STRUCTURE AND FUNCTION OF THE ESCHERICHIA COLI RIBONUCLEOTIDE REDUCTASE PROTEIN R2 Deposited 1993-01-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Not recorded FEO MU-OXO-DIIRON × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1RNR AUTOCATALYTIC GENERATION OF DOPA IN THE ENGINEERED PROTEIN R2 F208Y FROM ESCHERICHIA COLI RIBONUCLEOTIDE REDUCTASE AND CRYSTAL STRUCTURE OF THE DOPA-208 PROTEIN Deposited 1993-04-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Chain B 2–376（375 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) FE FE (III) ION × 4 HG MERCURY (II) ION × 14 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1RSR azide complex of the diferrous F208A mutant R2 subunit of ribonucleotide reductase Deposited 2003-12-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Mutation：Y122F, F208A Mutation：Y122F, F208A FE2 FE (II) ION × 4 HG MERCURY (II) ION × 12 AZI AZIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；100mM MES, 200mM NaCl, 1mM EMTS (Thimerosal), 16-24% PEG 4000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.289
1RSV azide complex of the diferrous E238A mutant R2 subunit of ribonucleotide reductase Deposited 2003-12-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Mutation：Y122F, E238A Mutation：Y122F, E238A FE FE (III) ION × 4 HG MERCURY (II) ION × 12 AZI AZIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；298 K；100mM MES, 200mM NaCl, 1mM EMTS (Thimerosal), 16-24% PEG 4000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.20 Å R-free 0.256
1XIK RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE 1 BETA CHAIN Deposited 1996-08-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa） Fragment：BETA CHAIN
Chain B 1–375（375 aa） Fragment：BETA CHAIN
Not recorded FE2 FE (II) ION × 4 HG MERCURY (II) ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；HANGING DROP VAPOR DIFFUSION METHOD, 20% PEG 4000, 0.2M NACL, 50MM MES BUFFER PH 6.0, 1MM ETHYLMERCURY SALICYLATE, vapor diffusion - hanging drop
Resolution 1.70 Å R-free 0.280
1YFD Crystal structure of the Y122H mutant of ribonucleotide reductase R2 protein from E. coli Deposited 2004-12-31 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–375（375 aa）
Chain B 1–375（375 aa）
Mutation：Y122H Mutation：Y122H HG MERCURY (II) ION × 13 FEO MU-OXO-DIIRON × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；295 K；PEG 4000, 0.1M MES, 0.4M NACL, 1mM EMTS, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Resolution 1.90 Å R-free 0.206
2ALX Ribonucleotide Reductase R2 from Escherichia coli in space group P6(1)22 Deposited 2005-08-08 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 0–339（340 aa） Fragment：residues 0-339
Not recorded MN MANGANESE (II) ION × 4 HG MERCURY (II) ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；ammonium sulfate, MES, manganese chloride, magnesium chloride, 4-(2-Hydroxyethyl)-1-piperazinepropanesulfonic acid, ethylmercurithiosalicylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.60 Å R-free 0.276
2AV8 Y122F MUTANT OF RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI Deposited 1997-09-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–340（340 aa）
Chain B 1–340（340 aa）
Mutation：Y122F Mutation：Y122F FE2 FE (II) ION × 1 FEO MU-OXO-DIIRON × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.6；PROTEIN WAS CRYSTALLIZED FROM 80% SATURATED NACL, NEAR PHYSIOLOGICAL PH (PH 7.6)
Resolution 2.46 Å R-free 0.237
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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain P 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
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 conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
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 conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
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 conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded No recorded non-water small molecule 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Chain E 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：RIBONUCLEOTIDE REDUCTASE R2-PEPTIDE, RESIDUES 357-376
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 357–376（20 aa） Fragment：R1 BINDING PEPTIDE
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 357–376（20 aa） Fragment：R1 BINDING PEPTIDE
Chain E 357–376（20 aa） Fragment：R1 BINDING PEPTIDE
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain P 357–376（20 aa） Fragment：R1 BINDING PEPTIDE
Not recorded 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
2XOF Ribonucleotide reductase Y122NO2Y modified R2 subunit of E. coli Deposited 2010-08-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Chain B 2–376（375 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) FEO MU-OXO-DIIRON × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.9；VAPOR DIFFUSION USING 90% OF SATURATED NACL, PH 7.9
Resolution 2.20 Å R-free 0.224
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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 2–376（375 aa）
Chain F 2–376（375 aa）
Chain G 2–376（375 aa）
Chain H 2–376（375 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 2–376（375 aa）
Chain F 2–376（375 aa）
Chain G 2–376（375 aa）
Chain H 2–376（375 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain F 2–376（375 aa）
Chain H 2–376（375 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 conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 2–376（375 aa）
Chain G 2–376（375 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain P 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 10 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain P 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain P 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 conditions Different structure-quality metrics Assembly 9 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 2–376（375 aa）
Chain F 2–376（375 aa）
Chain G 2–376（375 aa）
Chain H 2–376（375 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 2–376（375 aa）
Chain F 2–376（375 aa）
Chain G 2–376（375 aa）
Chain H 2–376（375 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 2–376（375 aa）
Chain F 2–376（375 aa）
Chain G 2–376（375 aa）
Chain H 2–376（375 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain E 2–376（375 aa）
Chain F 2–376（375 aa）
Chain G 2–376（375 aa）
Chain H 2–376（375 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain P 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 10 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 11 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 12 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain P 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 9 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 C 1–376（376 aa）
Chain D 1–376（376 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) 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
7AI9 Structure of Ribonucleotide reductase R2 from Escherichia coli collected by rotation serial crystallography on a COC membrane at a synchrotron source Deposited 2020-09-26 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–376（376 aa）
Not recorded FE FE (III) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；294 K；34-37 % PAA 2100, 100 mM HEPES 7.0, 250-450 mM NaCl, 200 mM ammonium sulfate [and] 26% PAA 2100, 100 mM HEPES 7.0, 150 NaCl, 100 Malonate
Resolution 2.00 Å R-free 0.191
7BET Structure of Ribonucleotide reductase R2 from Escherichia coli collected by femtosecond serial crystallography on a COC membrane Deposited 2020-12-24 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–376（376 aa）
Not recorded FE FE (III) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；294 K；34-37 % PAA 2100, 100 mM HEPES 7.0, 250-450 mM NaCl, 200 mM ammonium sulfate [and] 26% PAA 2100, 100 mM HEPES 7.0, 150 NaCl, 100 Malonate
Resolution 2.30 Å R-free 0.245
7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain P 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain F 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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 ligand/ion Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain D 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Chain E 356–375（20 aa） Fragment：C-TERMINAL PORTION, 20 RESIDUES
Not recorded 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
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 conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 342–376（35 aa）
Chain B 342–376（35 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 C 1–376（376 aa）
Chain D 1–376（376 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
9SIG XFEL structure of oxidised Ribonucleotide reductase R2a Y122F mutant from E. coli Deposited 2025-08-28 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Chain B 2–376（375 aa）
Mutation：Y122F Mutation：Y122F FE FE (III) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；pH 5.5；297 K；0.1M Bis-Tris pH 5.5, PEG 3350 25%
Resolution 1.90 Å R-free 0.185
9SIH XFEL structure of Ribonucleotide reductase R2a Y122F mutant from E. coli,reduced form Deposited 2025-08-28 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Chain B 2–376（375 aa）
Mutation：Y122F Mutation：Y122F FE2 FE (II) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；pH 5.5；297 K；0.1M Bis-Tris pH 5.5, PEG 3350 25%
Resolution 1.70 Å R-free 0.191
9SJW Serial electron diffraction (SerialED) structure of Y122F mutant Ribonucleotide reductase R2 from E. coli in its oxidised (met) form Deposited 2025-09-01 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Chain B 2–376（375 aa）
Not recorded FE FE (III) ION × 4 ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 5.5；Crystallization was performed using 23.5 uL protein solution, 25 mM HEPES-Na pH 7.0, 50 mM NaCl, and 20 uL crystallization buffer with seeds, 25 percent PEG 3350, 0.1 M Bis-Tris, pH 5.5.
cryo-EM vitrification conditions Cryogen ETHANE；Excess liquid was manually blotted from the backside for approximately 10 seconds, followed by plunge freezing in liquid ethane.
Resolution 1.80 Å R-free 0.234
9SJX Serial electron diffraction (SerialED) structure of Y122F mutant Ribonucleotide reductase R2 from E. coli in its oxidised (met) form (re-oxidised) Deposited 2025-09-01 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Chain B 2–376（375 aa）
Not recorded FE FE (III) ION × 4 ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 5.5；Crystallization was performed using 23.5 uL protein solution - 25 mM HEPES-Na pH 7.0, 50 mM NaCl and 50 mM sodium dithionite - and 20 uL crystallization buffer containing seeds, 25 percent PEG 3350, 0.1 M Bis-Tris pH 5.5 and 2 mM sodium dithioninte. The crystals were then oxidized through repeated wash with oxygen containing buffer of 12% PEG, 0.05 M Bis-Tris at pH 5.5.
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.00 Å R-free 0.285
9SJY Serial electron diffraction (SerialED) structure of Ribonucleotide reductase R2 from E. coli in its oxidised (met) form Deposited 2025-09-01 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Chain B 2–376（375 aa）
Not recorded FE FE (III) ION × 4 ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 5.5；Crystallization was performed using 23.5 uL protein solution, 25 mM HEPES-Na pH 7.0, 50 mM NaCl, and 20 uL crystallization buffer with seeds, 25 percent PEG 3350, 0.1 M Bis-Tris, pH 5.5.
cryo-EM vitrification conditions Cryogen ETHANE；Excess liquid was manually blotted from the backside for approximately 10 seconds, followed by plunge freezing in liquid ethane.
Resolution 1.80 Å R-free 0.253
9SJZ Serial electron diffraction (SerialED) structure of Ribonucleotide reductase R2 from E. coli in its oxidised (met) form (re-oxidised) Deposited 2025-09-01 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Chain B 2–376（375 aa）
Not recorded FE FE (III) ION × 4 ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 5.5；Crystallization was performed using 23.5 uL protein solution - 25 mM HEPES-Na pH 7.0, 50 mM NaCl and 50 mM sodium dithionite - and 20 uL crystallization buffer containing seeds, 25 percent PEG 3350, 0.1 M Bis-Tris pH 5.5 and 2 mM sodium dithioninte. The crystals were then oxidized through repeated wash with oxygen containing buffer of 12% PEG, 0.05 M Bis-Tris at pH 5.5.
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.70 Å R-free 0.232
9SK1 Serial electron diffraction (SerialED) structure of Y122F mutant Ribonucleotide reductase R2 from E. coli in its reduced (red) form Deposited 2025-09-01 Different construct Different mutation/modification 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 2–376（375 aa）
Chain B 2–376（375 aa）
Not recorded FE2 FE (II) ION × 4 ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 5.5；Crystallization was performed using 23.5 uL protein solution - 25 mM HEPES-Na pH 7.0, 50 mM NaCl and 50 mM sodium dithionite - and 20 uL crystallization buffer containing seeds, 25 percent PEG 3350, 0.1 M Bis-Tris pH 5.5 and 2 mM sodium dithioninte.
cryo-EM vitrification conditions Cryogen ETHANE；Excess liquid was manually blotted from the backside for approximately 10 seconds, followed by plunge freezing in liquid ethane. Sample was prepared in an inert environment within a glove box.
Resolution 1.80 Å R-free 0.222
9SKG Serial electron diffraction (SerialED) structure of Ribonucleotide reductase R2 from E. coli in its reduced (red) form Deposited 2025-09-02 Different construct Different mutation/modification 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 2–376（375 aa）
Chain B 2–376（375 aa）
Not recorded FE2 FE (II) ION × 4 ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 5.5；Crystallization was performed using 23.5 uL protein solution - 25 mM HEPES-Na pH 7.0, 50 mM NaCl and 50 mM sodium dithionite - and 20 uL crystallization buffer containing seeds, 25 percent PEG 3350, 0.1 M Bis-Tris pH 5.5 and 2 mM sodium dithioninte.
cryo-EM vitrification conditions Cryogen ETHANE；Excess liquid was manually blotted from the backside for approximately 10 seconds, followed by plunge freezing in liquid ethane. Sample was prepared in an inert environment within a glove box.
Resolution 1.80 Å R-free 0.247
9TCD XFEL structure of oxidised Ribonucleotide reductase R2a Y122F mutant from E. coli, hexagonal P6122 form Deposited 2025-11-21 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Mutation：Y122F FE FE (III) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；297 K；4M Sodium Formate
Resolution 2.70 Å R-free 0.254
9TCE XFEL structure of Ribonucleotide reductase R2a Y122F mutant from E. coli,reduced form, hexagonal P6122 Deposited 2025-11-21 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 2–376（375 aa）
Mutation：Y122F FE2 FE (II) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；297 K；4M Sodium Formate
Resolution 2.70 Å R-free 0.281

62 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RIR2_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–376； UniProt 1–376

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 7ai8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ai8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ai8
Deposition date deposition_date2020-09-26
Structure title titleStructure of Ribonucleotide reductase R2 from Escherichia coli collected by still serial crystallography on a COC membrane at a synchrotron source
Keywords keywordsmetalloprotein, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier22.07 Å
Radius of gyration Rg (electron density) rg_electron20.93 Å
Forward intensity I(0) i026046200.00
Molecular weight molecular_weight39543.0 kDa
Excluded volume excluded_volume49604 ų
Envelope volume envelope_volume56673 ų
Hydration-shell volume shell_volume22586 ų
Envelope diameter envelope_diameter71.5 Å
Shell Rg shell_rg27.83 Å
Envelope Rg envelope_rg21.37 Å
Shape Rg shape_rg20.93 Å
Total Rg total_rg21.79 Å
Total atoms total_atoms2783
Residues n_residues339
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 dmax71.9 Å
Rg (real space) rg_real22.03 Å
Rg uncertainty (real space) rg_real_error0.47 Å
I(0) (real space) i0_real2.6050e+07
I(0) uncertainty (real space) i0_real_error3.3870e+05
Rg (reciprocal space) rg_reciprocal22.04 Å
I(0) (reciprocal space) i0_reciprocal26050000.0000
Solution quality estimate total_estimate0.8887
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.8 Å
Skewness Skewness skewness0.322
Kurtosis Kurtosis kurtosis-0.382
Angular range angular_range— – 0.3600 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5244000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.976
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7ai8A01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology620 — Ribonucleotide Reductase, subunit A
Homologous superfamily homologous superfamily20 — Ribonucleotide Reductase, subunit A
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8. Citations (1)

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9. Files and Curves (10)