Current Protein Identity:P07276 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
2LOX NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and Rad2 Deposited 2012-01-27 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 642–690(49 aa) Fragment:UNP residues 642-690
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5;300 K;Pressure ambient
NMR sample composition 1 mM [U-100% 13C; U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-100% 13C; U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 100% D2O | 100% D2O
NMR sample composition 1 mM [U-100% 15N] Tfb1, 1.25 mM Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.25 mM Tfb1, 1 mM [U-100% 13C; U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.25 mM Tfb1, 1 mM [U-100% 13C; U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 100% D2O | 100% D2O
NMR sample composition 1.25 mM Tfb1, 1 mM [U-100% 15N] Rad2, 20 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
4Q0R The catalytic core of Rad2 (complex I) Deposited 2014-04-02 Assembly 1 Protein–DNA Monomer;Protein × 1 PDB declaration: dimeric(2) Consistent with all polymers
Chain A 2–111(110 aa) Fragment:enzyme catalytic core, unp residues 2-111, unp residues 732-986
Chain A 732–986(255 aa) Fragment:enzyme catalytic core, unp residues 2-111, unp residues 732-986
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 VAPOR DIFFUSION, SITTING DROP;291 K;20% (v/v) ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.75 Å R-free 0.310
4Q0R The catalytic core of Rad2 (complex I) Deposited 2014-04-02 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 2–111(110 aa) Fragment:enzyme catalytic core, unp residues 2-111, unp residues 732-986
Chain B 732–986(255 aa) Fragment:enzyme catalytic core, unp residues 2-111, unp residues 732-986
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 VAPOR DIFFUSION, SITTING DROP;291 K;20% (v/v) ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.75 Å R-free 0.310
4Q0W he catalytic core of Rad2 in complex with DNA substrate (complex II) Deposited 2014-04-02 Assembly 1 Protein–DNA Homooligomer;Protein × 2 PDB declaration: tetrameric(4) Consistent with all polymers
Chain A 2–111(110 aa) Fragment:Rad2
Chain A 732–986(255 aa) Fragment:Rad2
Chain B 2–111(110 aa) Fragment:Rad2
Chain B 732–986(255 aa) Fragment:Rad2
Not recorded CA CALCIUM ION × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;9% (w/v) PEG 20000, 20% (v/v) PEG MME 550, 0.2 M D-glucose, 0.2 M D-mannose, 0.2 M D-galactose, 0.2 M L-fructose, 0.2 M D-xylose, 0.2 M N-acetyl-D-glucosamine, and 0.1 M MOPS/HEPES-Na, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.10 Å R-free 0.230
4Q0Z The catalytic core of Rad2 in complex with DNA substrate (complex III) Deposited 2014-04-02 Assembly 1 Protein–DNA Homooligomer;Protein × 2 PDB declaration: tetrameric(4) Consistent with all polymers
Chain A 2–111(110 aa) Fragment:Rad2 catalytic core
Chain A 732–986(255 aa) Fragment:Rad2 catalytic core
Chain B 2–111(110 aa) Fragment:Rad2 catalytic core
Chain B 732–986(255 aa) Fragment:Rad2 catalytic core
Not recorded CA CALCIUM ION × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;10% (w/v) PEG 8000, 20% (v/v) ethylene glycol, 0.2 M D-glucose, 0.2 M D-mannose, 0.2 M D-galactose, 0.2 M L-fructose, 0.2 M D-xylose, 0.2 M N-acetyl-D-glucosamine, and 0.1 M MES/imidazole, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.40 Å R-free 0.235
4Q0Z The catalytic core of Rad2 in complex with DNA substrate (complex III) Deposited 2014-04-02 Assembly 2 Protein–DNA Homooligomer;Protein × 2 PDB declaration: tetrameric(4) Consistent with all polymers
Chain E 2–111(110 aa) Fragment:Rad2 catalytic core
Chain E 732–986(255 aa) Fragment:Rad2 catalytic core
Chain F 2–111(110 aa) Fragment:Rad2 catalytic core
Chain F 732–986(255 aa) Fragment:Rad2 catalytic core
Not recorded CA CALCIUM ION × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;10% (w/v) PEG 8000, 20% (v/v) ethylene glycol, 0.2 M D-glucose, 0.2 M D-mannose, 0.2 M D-galactose, 0.2 M L-fructose, 0.2 M D-xylose, 0.2 M N-acetyl-D-glucosamine, and 0.1 M MES/imidazole, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.40 Å R-free 0.235
4Q10 The catalytic core of Rad2 in complex with DNA substrate (complex IV) Deposited 2014-04-02 Assembly 1 Protein–DNA Homooligomer;Protein × 2 PDB declaration: tetrameric(4) Consistent with all polymers
Chain A 2–111(110 aa) Fragment:enzyme catalytic core, unp residues 2-111, unp residues 732-986
Chain A 732–986(255 aa) Fragment:enzyme catalytic core, unp residues 2-111, unp residues 732-986
Chain B 2–111(110 aa) Fragment:enzyme catalytic core, unp residues 2-111, unp residues 732-986
Chain B 732–986(255 aa) Fragment:enzyme catalytic core, unp residues 2-111, unp residues 732-986
Not recorded CA CALCIUM ION × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7.5;291 K;8% (w/v) PEG 8000, 18% (v/v) ethylene glycol, 0.2 M D-glucose, 0.2 M D-mannose, 0.2 M D-galactose, 0.2 M L-fructose, 0.2 M D-xylose, 0.2 M N-acetyl-D-glucosamine, and 0.1 M MOPS/HEPES-Na, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.70 Å R-free 0.284