Current Protein Identity:P46013 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
1R21 Solution Structure of human Ki67 FHA Domain Deposited 2003-09-25 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–120(120 aa) Fragment:FHA domain
Mutation:none No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 8.4;290 K;Ionic strength (raw mmCIF value) 0;Pressure ambient
NMR measurement conditions pH 7.5;290 K;Ionic strength (raw mmCIF value) 150 mM NaCl;Pressure ambient
NMR sample composition 0.5 mM U-13C,15N-protein; 10 mM TrisHCl buffer (pH 8.4); 2mM DTT; 1 mM EDTA | 95% H2O, 10% D2O
NMR sample composition 0.5 mM U-13C,15N-protein; 5 mM HEPES buffer (pH 7.5); 2mM DTT; 1 mM EDTA; 150 mM NaCl | 95% H2O, 10% D2O
NMR sample composition 0.5 mM unlabeled-protein; 10 mM TrisHCl buffer (pH 8.4); 2mM DTT; 1 mM EDTA | 95% H2O, 10% D2O
NMR sample composition 0.5 mM unlabeled-protein; 10 mM TrisHCl buffer (pH 8.4); 2mM DTT; 1 mM EDTA | 100% D2O
Resolution not provided
2AFF The solution structure of the Ki67FHA/hNIFK(226-269)3P complex Deposited 2005-07-25 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 1–120(120 aa) Fragment:FHA domain
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4;293 K;Ionic strength (raw mmCIF value) 150 mM NaCl;Pressure ambient
NMR sample composition 0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 93% H2O/7% D2O
NMR sample composition 0.9 mM Ki67 FHA U-15N,13C; 1 mM hNIFK(226-269)3P unlabeled 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 100% D2O
NMR sample composition 1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 93% H2O/7% D2O
NMR sample composition 1 mM Ki67 FHA unlabled; 0.9 mM hNIFK(226-269)3P U-15N,13C 5 mM HEPES, 5 mM DTT, 1 mM EDTA, 150 mM NaCl, pH 7.4 | 100% D2O
Resolution not provided
5J28 Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex Deposited 2016-03-29 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 496–536(41 aa) Fragment:UNP residues 496-536
Mutation:T525M MLI MALONATE ION × 1 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 4;277 K;1.9 M Sodium Malonate pH 4.0
Resolution 2.00 Å R-free 0.197
5J28 Ki67-PP1g (protein phosphatase 1, gamma isoform) holoenzyme complex Deposited 2016-03-29 Assembly 2 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain D 496–536(41 aa) Fragment:UNP residues 496-536
Mutation:T525M MLI MALONATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 4;277 K;1.9 M Sodium Malonate pH 4.0
Resolution 2.00 Å R-free 0.197