Current Protein Identity:P11157 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1AFT SMALL SUBUNIT C-TERMINAL INHIBITORY PEPTIDE OF MOUSE RIBONUCLEOTIDE REDUCTASE AS BOUND TO THE LARGE SUBUNIT, NMR, 26 STRUCTURES Deposited 1997-03-13 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 384–390(7 aa) Fragment:C-TERMINAL RESIDUES AC-FTLDADF OF SMALL SUBUNIT
Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7;287 K
Resolution not provided
1H0N Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state Deposited 2002-06-26 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–390(390 aa)
Not recorded CO COBALT (II) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6;0.1 M NA-ACETATE BUFFER PH4.7, 1.2 M NACL, 7.5 MG/ML APO-R2 PROTEIN. CRYSTALS WERE SOAKED IN 5 MM CO2+ SOLUTION, PH INCREASED TO 6
Resolution 2.40 Å R-free 0.297
1H0O Cobalt substitution of mouse R2 ribonucleotide reductase to model the reactive diferrous state Deposited 2002-06-26 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–390(390 aa)
Not recorded CO COBALT (II) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.7;0.1 M NA-ACETATE BUFFER PH4.7, 1.2 M NACL, 7.5 MG/ML APO-R2 PROTEIN. CRYSTALS WERE MADE BY CO-CRYSTALLISATION (3.8 EQV. CO2+)., pH 4.70
Resolution 2.20 Å R-free 0.282
1W68 Crystal Structure of Mouse Ribonucleotide Reductase Subunit R2 under Oxidizing Conditions. A Fully Occupied Dinuclear Iron Cluster. Deposited 2004-08-16 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–390(390 aa)
Not recorded FEO MU-OXO-DIIRON × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6;0.1 M SODIUM ACETATE PH 4.7, 1.2 M SODIUM CHLORIDE
Resolution 2.20 Å R-free 0.260
1W69 Crystal Structure of Mouse Ribonucleotide Reductase Subunit R2 under Reducing Conditions. A Fully Occupied Dinuclear Iron Cluster and Bound Acetate. Deposited 2004-08-16 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–390(390 aa)
Not recorded FE2 FE (II) ION × 4 ACY ACETIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6;0.1 M SODIUM ACETATE PH 4.7, 1.2 M SODIUM CHLORIDE
Resolution 2.20 Å R-free 0.272
1XSM PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE FROM MOUSE Deposited 1996-07-03 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–390(390 aa)
Not recorded FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 4.7;1.0-1.2 M NACL, 0.1 M SODIUM ACETATE, PH 4.7, 0-4% PEG4000.
Resolution 2.30 Å R-free 0.250