Ribonucleoside-diphosphate reductase 1 subunit alpha
Escherichia coli (strain K12)
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count | Chain A； UniProt 1–761 Chain B； UniProt 1–761 | Not recorded | Ribonucleoside-diphosphate reductase 1 subunit beta × 2 （P69924） 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 |
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 6W4X | Assembly / Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Non-polymers | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|---|
| 1QFN GLUTAREDOXIN-1-RIBONUCLEOTIDE REDUCTASE B1 MIXED DISULFIDE BOND Deposited 1999-04-12 | 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 × 2 PDB declaration: dimeric |
Chain B
737–761（25 aa）
Fragment：apha chain, B1 SUBUNIT
|
Mutation：C754S | No recorded non-water small molecule |
SOLUTION NMR
NMR measurement conditions
pH 6.5；293 K；Pressure 1
|
Resolution not provided |
| 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 method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
1–761（761 aa）
|
Mutation：Y730F | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 2.90 Å R-free 0.245 |
| 1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
1–761（761 aa）
|
Mutation：Y730F | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 2.90 Å R-free 0.245 |
| 1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
1–761（761 aa）
|
Mutation：Y730F | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 2.90 Å R-free 0.245 |
| 1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：Y730F Mutation：Y730F | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 2.90 Å R-free 0.245 |
| 1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
|
Mutation：Y730F | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 2.90 Å R-free 0.245 |
| 1R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN MUTANT Y730F WITH A REDUCED ACTIVE SITE FROM ESCHERICHIA COLI Deposited 1997-07-15 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：Y730F Mutation：Y730F | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 2.90 Å R-free 0.245 |
| 1RLR STRUCTURE OF RIBONUCLEOTIDE REDUCTASE PROTEIN R1 Deposited 1994-08-12 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric |
Chain A
1–761（761 aa）
|
Not recorded | No recorded non-water small molecule | X-RAY DIFFRACTION mmCIF provides none of the parsed conditions | Resolution 2.50 Å |
| 2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
1–761（761 aa）
|
Not recorded | TTP THYMIDINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.280 |
| 2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
1–761（761 aa）
|
Not recorded | TTP THYMIDINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.280 |
| 2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
1–761（761 aa）
|
Not recorded | TTP THYMIDINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.280 |
| 2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | TTP THYMIDINE-5'-TRIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.280 |
| 2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
|
Not recorded | TTP THYMIDINE-5'-TRIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.280 |
| 2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | TTP THYMIDINE-5'-TRIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.280 |
| 2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain C
1–761（761 aa）
|
Not recorded | TTP THYMIDINE-5'-TRIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.280 |
| 2R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH DTTP OCCUPYING THE SPECIFICITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
1–761（761 aa）
|
Not recorded | TTP THYMIDINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.280 |
| 2X0X Ribonucleotide reductase R1 subunit of E. coli to 2.3 A resolution Deposited 2009-12-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
|
Not recorded | SO4 SULFATE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE APP 1.5M, SODIUM CITRATE BUFFER PH APP 6.
|
Resolution 2.30 Å R-free 0.224 |
| 2X0X Ribonucleotide reductase R1 subunit of E. coli to 2.3 A resolution Deposited 2009-12-18 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | SO4 SULFATE ION × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE APP 1.5M, SODIUM CITRATE BUFFER PH APP 6.
|
Resolution 2.30 Å R-free 0.224 |
| 2XAK Ribonucleotide reductase Y730NO2Y modified R1 subunit of E. coli Deposited 2010-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.80 Å R-free 0.241 |
| 2XAK Ribonucleotide reductase Y730NO2Y modified R1 subunit of E. coli Deposited 2010-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.80 Å R-free 0.241 |
| 2XAP Ribonucleotide reductase Y731NO2Y modified R1 subunit of E. coli to 2. 1 A resolution Deposited 2010-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.10 Å R-free 0.230 |
| 2XAP Ribonucleotide reductase Y731NO2Y modified R1 subunit of E. coli to 2. 1 A resolution Deposited 2010-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.10 Å R-free 0.230 |
| 2XAV Ribonucleotide reductase Y731NO2Y and Y730F modified R1 subunit of E. coli Deposited 2010-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.80 Å R-free 0.247 |
| 2XAV Ribonucleotide reductase Y731NO2Y and Y730F modified R1 subunit of E. coli Deposited 2010-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.80 Å R-free 0.247 |
| 2XAW Ribonucleotide reductase Y730NO2Y and Y731F modified R1 subunit of E. coli Deposited 2010-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 3.10 Å R-free 0.234 |
| 2XAW Ribonucleotide reductase Y730NO2Y and Y731F modified R1 subunit of E. coli Deposited 2010-03-31 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 3.10 Å R-free 0.234 |
| 2XAX Ribonucleotide reductase Y730NO2Y and Y731A modified R1 subunit of E. coli Deposited 2010-04-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.75 Å R-free 0.261 |
| 2XAX Ribonucleotide reductase Y730NO2Y and Y731A modified R1 subunit of E. coli Deposited 2010-04-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.75 Å R-free 0.261 |
| 2XAY Ribonucleotide reductase Y730NO2Y and C439A modified R1 subunit of E. coli Deposited 2010-04-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.65 Å R-free 0.235 |
| 2XAY Ribonucleotide reductase Y730NO2Y and C439A modified R1 subunit of E. coli Deposited 2010-04-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.65 Å R-free 0.235 |
| 2XAZ Ribonucleotide reductase Y730NO2Y and C439S modified R1 subunit of E. coli Deposited 2010-04-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.60 Å R-free 0.246 |
| 2XAZ Ribonucleotide reductase Y730NO2Y and C439S modified R1 subunit of E. coli Deposited 2010-04-01 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Mutation：YES Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.60 Å R-free 0.246 |
| 2XO4 RIBONUCLEOTIDE REDUCTASE Y730NH2Y MODIFIED R1 SUBUNIT OF E. COLI Deposited 2010-08-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.50 Å R-free 0.233 |
| 2XO4 RIBONUCLEOTIDE REDUCTASE Y730NH2Y MODIFIED R1 SUBUNIT OF E. COLI Deposited 2010-08-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：RESIDUES 1-761
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.50 Å R-free 0.233 |
| 2XO5 RIBONUCLEOTIDE REDUCTASE Y731NH2Y MODIFIED R1 SUBUNIT OF E. COLI Deposited 2010-08-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
Fragment：CATALYTIC SUBUNIT, RESIDUES 1-761
|
Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.70 Å R-free 0.228 |
| 2XO5 RIBONUCLEOTIDE REDUCTASE Y731NH2Y MODIFIED R1 SUBUNIT OF E. COLI Deposited 2010-08-09 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Fragment：CATALYTIC SUBUNIT, RESIDUES 1-761
Chain B
1–761（761 aa）
Fragment：CATALYTIC SUBUNIT, RESIDUES 1-761
|
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；LITHIUM SULPHATE 1.5M, SODIUM CHLORIDE BUFFER PH 6.
|
Resolution 2.70 Å R-free 0.228 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 7 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 8 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH AMPPNP OCCUPYING THE ACTIVITY SITE FROM ESCHERICHIA COLI Deposited 1997-07-21 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 9 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM AMPPNP AND 10 MM CDP WAS ALSO INCLUDED IN THE PROTEIN SOLUTION
|
Resolution 3.00 Å R-free 0.287 |
| 3UUS Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex Deposited 2011-11-28 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
Chain C
1–761（761 aa）
Chain D
1–761（761 aa）
|
Not recorded | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 8 FE FE (III) ION × 8 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；10.8% PEG 3350, 0.18M magnesium acetate, 0.09M MOPS pH 7.5, 0.01M iron (III) chloride, 4.5% glycerol , VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 5.65 Å R-free 0.303 |
| 4ERM Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex at 4 Angstroms resolution Deposited 2012-04-20 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
Chain C
1–761（761 aa）
Chain D
1–761（761 aa）
|
Not recorded | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 8 DAT 2'-DEOXYADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 FEO MU-OXO-DIIRON × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Precipitant conditions: 10% PEG 3350, 0.1 M MOPS pH 7.5, 0.2 M Magnesium Acetate, 0.025 M Magnesium Chloride, 0.006 M n-Nonyl-beta-D-maltopyranoside, and 5% glycerol. Mixed 1:1 with protein., VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 3.95 Å R-free 0.284 |
| 4ERP Crystal structure of a gemcitabine-diphosphate inhibited E. coli class Ia ribonucleotide reductase complex Deposited 2012-04-20 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 4 FEO MU-OXO-DIIRON × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Precipitant solution: 25% PEG 3350, 0.1 M HEPES pH 7.5, 0.2 M ammonium acetate, 5% glycerol mixed 2:1 with protein and streak seeded from crystals grown under similar conditions. , VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 4.45 Å R-free 0.267 |
| 4ERP Crystal structure of a gemcitabine-diphosphate inhibited E. coli class Ia ribonucleotide reductase complex Deposited 2012-04-20 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain C
1–761（761 aa）
Chain D
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 4 FEO MU-OXO-DIIRON × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；Precipitant solution: 25% PEG 3350, 0.1 M HEPES pH 7.5, 0.2 M ammonium acetate, 5% glycerol mixed 2:1 with protein and streak seeded from crystals grown under similar conditions. , VAPOR DIFFUSION, HANGING DROP, temperature 298K
|
Resolution 4.45 Å R-free 0.267 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
1–761（761 aa）
|
Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 10 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
1–761（761 aa）
|
Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
1–761（761 aa）
|
Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
1–761（761 aa）
|
Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 15 PDB declaration: pentadecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：C292A Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
|
Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：C292A Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain C
1–761（761 aa）
|
Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 8 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：C292A Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 6 GDP GUANOSINE-5'-DIPHOSPHATE × 6 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 4R1R RIBONUCLEOTIDE REDUCTASE R1 PROTEIN WITH SUBSTRATE, GDP AND EFFECTOR DTTP FROM ESCHERICHIA COLI Deposited 1997-07-22 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 9 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：C292A Mutation：C292A | TTP THYMIDINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0. THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20-FOLD EXCESS FO A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION. 10 MM DTTP AND 10 MM GDP WAS ADDED TO THE PROTEIN SOLUTION 48 H BEFORE FREEZING THE PROTEIN CRYSTALS
|
Resolution 3.20 Å R-free 0.308 |
| 5CNS Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to CDP and dATP at 2.97 Angstroms resolution Deposited 2015-07-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
Chain C
1–761（761 aa）
Chain D
1–761（761 aa）
|
Not recorded | CDP CYTIDINE-5'-DIPHOSPHATE × 4 DAT 2'-DEOXYADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 8 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 FEO MU-OXO-DIIRON × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；9.5% (w/v) PEG 3350, 100 mM MOPS, 250 mM Mg(CH3COO)2, 25 mM
394 MgCl2, 5% (v/v) glycerol
|
Resolution 2.98 Å R-free 0.214 |
| 5CNT Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to UDP and dATP at 3.25 Angstroms resolution Deposited 2015-07-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
Chain C
1–761（761 aa）
Chain D
1–761（761 aa）
|
Not recorded | UDP URIDINE-5'-DIPHOSPHATE × 4 DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 8 FEO MU-OXO-DIIRON × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2% (w/v) PEG 3350, 100 mM MOPS pH 7.5, 300 mM Mg(CH3COO)2, 30 mM MgCl2, and 5% (v/v) glycerol
|
Resolution 3.25 Å R-free 0.221 |
| 5CNU Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to ADP and dGTP at 3.40 Angstroms resolution Deposited 2015-07-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
Chain C
1–761（761 aa）
Chain D
1–761（761 aa）
|
Not recorded | DGT 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 4 DAT 2'-DEOXYADENOSINE-5'-DIPHOSPHATE × 4 FEO MU-OXO-DIIRON × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2% (w/v) PEG 3350, 100 mM MOPS pH 7.5, 300 mM Mg(CH3COO)2, 30 mM MgCl2, and 5% (v/v) glycerol
|
Resolution 3.40 Å R-free 0.221 |
| 5CNV Crystal structure of the dATP inhibited E. coli class Ia ribonucleotide reductase complex bound to GDP and TTP at 3.20 Angstroms resolution Deposited 2015-07-18 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
Chain C
1–761（761 aa）
Chain D
1–761（761 aa）
|
Not recorded | GDP GUANOSINE-5'-DIPHOSPHATE × 4 DAT 2'-DEOXYADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 8 TTP THYMIDINE-5'-TRIPHOSPHATE × 8 FEO MU-OXO-DIIRON × 4 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；2% (w/v) PEG 3350, 100 mM MOPS pH 7.5, 300 mM Mg(CH3COO)2, 30 mM MgCl2, and 5% (v/v) glycerol
|
Resolution 3.20 Å R-free 0.219 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 10 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441A Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 11 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain C
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 12 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441A Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric |
Chain B
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 7 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric |
Chain A
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 8 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric |
Chain C
1–761（761 aa）
|
Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 5R1R RIBONUCLEOTIDE REDUCTASE E441A MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 9 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441A Mutation：E441A | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.227 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
1–761（761 aa）
|
Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
1–761（761 aa）
|
Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
1–761（761 aa）
|
Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441D Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
|
Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441D Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441D Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 8 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain C
1–761（761 aa）
|
Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 6R1R RIBONUCLEOTIDE REDUCTASE E441D MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 9 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain A
1–761（761 aa）
|
Mutation：E441D | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.240 |
| 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 method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric |
Chain A
1–761（761 aa）
|
Mutation：E441Q | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.231 |
| 7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain B
1–761（761 aa）
|
Mutation：E441Q | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.231 |
| 7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric |
Chain C
1–761（761 aa）
|
Mutation：E441Q | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.231 |
| 7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain C
1–761（761 aa）
|
Mutation：E441Q | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.231 |
| 7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 5 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441Q Mutation：E441Q | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.231 |
| 7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 6 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441Q Mutation：E441Q | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.231 |
| 7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 7 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain C
1–761（761 aa）
|
Mutation：E441Q | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.231 |
| 7R1R RIBONUCLEOTIDE REDUCTASE E441Q MUTANT R1 PROTEIN FROM ESCHERICHIA COLI Deposited 1997-09-17 | Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 8 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Mutation：E441Q Mutation：E441Q | No recorded non-water small molecule |
X-RAY DIFFRACTION
X-ray crystallization conditions
pH 6；PROTEIN WAS CRYSTALLIZED FROM 1.7 M LITHIUM SULFATE, AND 10 MM MAGNESIUM SULFATE IN 25 MM CITRATE BUFFER AT PH 6.0 THE PROTEIN SOLUTION CONTAINED 17 MG/ML R1 PROTEIN, 20 FOLD EXCESS OF A 20-RESIDUE PEPTIDE CORRESPONDING TO THE C-TERMINUS OF THE R2 SUBUNIT AND IS ESSENTIAL FOR CRYSTALLIZATION
|
Resolution 3.10 Å R-free 0.231 |
| 8VHN Crystal Structure of E. coli class Ia ribonucleotide reductase alpha subunit bound to two ATP molecules Deposited 2024-01-02 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 GOL GLYCEROL × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；293.15 K；8.0% (w/vol)PEG3350, 80 mM HEPES pH 7.3, 280 mM magnesium chloride, 4% (vol/vol) glycerol, 1.0% CYMAL-1 detergent
|
Resolution 2.62 Å R-free 0.209 |
| 8VHO Crystal Structure of E. coli class Ia ribonucleotide reductase alpha subunit bound to dATP Deposited 2024-01-02 | Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 GOL GLYCEROL × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；277.15 K；6.8% (w/vol) PEG3350, 80mM HEPES pH7.3, 280mM MgCl2, 4% (vol/vol) glycerol, and 1.0% CYMAL-1 detergent
|
Resolution 2.55 Å R-free 0.205 |
| 8VHP Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to CDP and two molecules of ATP Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–760（760 aa）
Chain B
1–760（760 aa）
|
Mutation：W28A Mutation：W28A | SO4 SULFATE ION × 12 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 CDP CYTIDINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291.15 K；1.9 M ammonium sulfate, 4% (w/vol) PEG MME 500, 0.1 M bis-Tris pH 6.5
|
Resolution 2.61 Å R-free 0.209 |
| 8VHP Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to CDP and two molecules of ATP Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
1–760（760 aa）
Chain D
1–760（760 aa）
|
Mutation：W28A Mutation：W28A | SO4 SULFATE ION × 12 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 CDP CYTIDINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291.15 K；1.9 M ammonium sulfate, 4% (w/vol) PEG MME 500, 0.1 M bis-Tris pH 6.5
|
Resolution 2.61 Å R-free 0.209 |
| 8VHP Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to CDP and two molecules of ATP Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 3 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain E
1–760（760 aa）
Chain F
1–760（760 aa）
|
Mutation：W28A Mutation：W28A | SO4 SULFATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 CDP CYTIDINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291.15 K；1.9 M ammonium sulfate, 4% (w/vol) PEG MME 500, 0.1 M bis-Tris pH 6.5
|
Resolution 2.61 Å R-free 0.209 |
| 8VHP Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to CDP and two molecules of ATP Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 4 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain G
1–760（760 aa）
Chain H
1–760（760 aa）
|
Mutation：W28A Mutation：W28A | SO4 SULFATE ION × 8 ATP ADENOSINE-5'-TRIPHOSPHATE × 6 MG MAGNESIUM ION × 4 CDP CYTIDINE-5'-DIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, HANGING DROP；291.15 K；1.9 M ammonium sulfate, 4% (w/vol) PEG MME 500, 0.1 M bis-Tris pH 6.5
|
Resolution 2.61 Å R-free 0.209 |
| 8VHQ Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and ATP Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–760（760 aa）
Chain B
1–760（760 aa）
|
Mutation：W28A Mutation：W28A | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；277.15 K；6.5-7.0% (w/vol) PEG3350, 0.1M HEPES 7.0, 0.35M MgSO4, 5% (vol/vol) glycerol.
|
Resolution 3.40 Å R-free 0.233 |
| 8VHQ Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and ATP Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
1–760（760 aa）
Chain D
1–760（760 aa）
|
Mutation：W28A Mutation：W28A | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；277.15 K；6.5-7.0% (w/vol) PEG3350, 0.1M HEPES 7.0, 0.35M MgSO4, 5% (vol/vol) glycerol.
|
Resolution 3.40 Å R-free 0.233 |
| 8VHR Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and GTP Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–760（760 aa）
Chain B
1–760（760 aa）
|
Mutation：W28A Mutation：W28A | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；277.15 K；6.5-7.0% (w/vol) PEG3350, 0.1M HEPES 7.0, 0.35M MgSO4, 5% (vol/vol) glycerol
|
Resolution 3.55 Å R-free 0.243 |
| 8VHR Crystal structure of E. coli class Ia ribonucleotide reductase alpha subunit W28A variant bound to dATP and GTP Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain C
1–760（760 aa）
Chain D
1–760（760 aa）
|
Mutation：W28A Mutation：W28A | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 4 MG MAGNESIUM ION × 4 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；277.15 K；6.5-7.0% (w/vol) PEG3350, 0.1M HEPES 7.0, 0.35M MgSO4, 5% (vol/vol) glycerol
|
Resolution 3.55 Å R-free 0.243 |
| 8VHU Crystal structure of dATP bound E. coli class Ia ribonucleotide reductase alpha construct fused with the C-terminal tail of E. coli class Ia beta subunit Deposited 2024-01-02 | Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics | Assembly 1 Insufficient information Homooligomer；Protein × 2 PDB declaration: dimeric |
Chain A
1–734（734 aa）
Chain B
1–734（734 aa）
|
Mutation：Truncated final 8 residues of alpha,fused C-terminal 35 residues of beta Mutation：Truncated final 8 residues of alpha,fused C-terminal 35 residues of beta | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 3 NA SODIUM ION × 1 CL CHLORIDE ION × 6 GOL GLYCEROL × 1 |
X-RAY DIFFRACTION
X-ray crystallization conditions
VAPOR DIFFUSION, SITTING DROP；277.15 K；1.4M NaCl, 8% (w/vol) PEG 6000
|
Resolution 2.10 Å R-free 0.192 |
| 9DB2 Class Ia ribonucleotide reductase with mechanism-based inhibitor N3CDP Deposited 2024-08-23 | Different ligand/ion Different experimental conditions Different structure-quality metrics | Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric |
Chain A
1–761（761 aa）
Chain B
1–761（761 aa）
|
Not recorded | DTP 2'-DEOXYADENOSINE 5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 UNL UNKNOWN LIGAND × 1 A1A3L 4-amino-1-{(3xi)-3-C-amino-2-deoxy-5-O-[(S)-hydroxy(phosphonooxy)phosphoryl]-beta-D-threo-pentofuranosyl}pyrimidin-2(1H)-one × 1 FEO MU-OXO-DIIRON × 2 |
ELECTRON MICROSCOPY
cryo-EM buffer
pH 7.6
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.60 Å |
33 other PDB entries and 104 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | RIR1_ECOLI |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A； PDBConstruct 1–761； UniProt 1–761 Author chain B； PDBConstruct 1–761； UniProt 1–761 |
