Current Protein Identity:Q05195 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state 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
1E91 Structure of the complex of the Mad1-Sin3B interaction domains Deposited 2000-10-04 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 8–20(13 aa) Fragment:SIN INTERACTION DOMAIN
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3;293 K
Resolution not provided
1NLW Crystal structure of Mad-Max recognizing DNA Deposited 2003-01-07 Assembly 1 Protein–DNA Heteromer;Protein × 2 PDB declaration: tetrameric(4) Consistent with all polymers
Chain A 57–136(80 aa) Fragment:bHLHZ region
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6;288 K;20% MPD, 5mM magnesium chloride, 50 mM sodium cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 2.00 Å R-free 0.324
1NLW Crystal structure of Mad-Max recognizing DNA Deposited 2003-01-07 Assembly 2 Protein–DNA Heteromer;Protein × 2 PDB declaration: tetrameric(4) Consistent with all polymers
Chain D 57–136(80 aa) Fragment:bHLHZ region
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6;288 K;20% MPD, 5mM magnesium chloride, 50 mM sodium cacodylate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 2.00 Å R-free 0.324
1PD7 Extended SID of Mad1 bound to the PAH2 domain of mSin3B Deposited 2003-05-19 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 5–28(24 aa) Fragment:extended SID domain (residues 5-28)
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3;293 K;Ionic strength (raw mmCIF value) 50 mM K2HPO4/KH2PO4;Pressure ambient
NMR sample composition 1.3 mM PAH2 U-15,13C; 1.3 mM SID 50 mM phosphate buffer pH 6.3 trace amounts of NaN3 and Pefabloc | 95% H20, 5% D20
Resolution not provided
1S5Q Solution Structure of Mad1 SID-mSin3A PAH2 Complex Deposited 2004-01-21 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 6–21(16 aa) Fragment:Sin3 Interaction Domain (SID), Residues 6 to 21
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6;300 K;Ionic strength (raw mmCIF value) 20 mM sodium phosphate, pH 6, 0.2% NaN3;Pressure ambient
NMR sample composition 1.0 mM 1:1 SID UNLABELED, PAH2 U-15N | 90% H2O/10% D2O
NMR sample composition 1.6 mM 1:1 SID UNLABELED, PAH2 U-15N,U-13C | 100% D2O
Resolution not provided