Current Protein Identity:P37613 New Search
Main Difference Dimensions in This Set
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
2K5T Solution NMR Structure of Putative N-Acetyl Transferase YhhK from E. coli Bound to Coenzyme A: Northeast Structural Genomics Consortium Target ET106 Deposited 2008-06-30 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–127(127 aa)
Mutation:A119T COA COENZYME A × 1 SOLUTION NMR
NMR measurement conditions pH 7;293 K;Ionic strength (raw mmCIF value) 300;Pressure ambient
NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] YhhK, 5 mM Coenzyme A, 7 % D2O, 300 mM sodium chloride, 25 mM TRIS, 5 mM DTT, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.6 mM [U-100% 13C; U-100% 15N] YhhK, 5 mM Coenzyme A, 100 % D2O, 300 mM sodium chloride, 25 mM TRIS, 5 mM DTT, 100% D2O | 100% D2O
Resolution not provided
4CRY Direct visualisation of strain-induced protein post-translational modification Deposited 2014-03-02 Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain B 1–127(127 aa)
Not recorded ACO ACETYL COENZYME *A × 4 MG MAGNESIUM ION × 4 CL CHLORIDE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.4;20% (W/V) POLYETHYLENE GLYCOL (PEG) 3350, 0.1 M BIS-TRIS PROPANE PH 7.4, 0.2 M POTASSIUM THIOCYANATE
Resolution 1.61 Å R-free 0.150
4CRZ Direct visualisation of strain-induced protein prost-translational modification Deposited 2014-03-02 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
Chain B 1–127(127 aa)
Not recorded SCN THIOCYANATE ION × 4 ACO ACETYL COENZYME *A × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.4;20% (W/V) POLYETHYLENE GLYCOL (PEG) 3350, 0.1 M BIS-TRIS PROPANE PH 7.4, 0.2 M POTASSIUM THIOCYANATE
Resolution 1.70 Å R-free 0.175
4CS0 Direct visualisation of strain-induced protein post-translational modification Deposited 2014-03-02 Assembly 1 Protein heterocomplex Heteromer;Protein × 8 PDB declaration: octameric(8) Consistent with protein count
Chain B 1–127(127 aa)
Not recorded SCN THIOCYANATE ION × 4 ACO ACETYL COENZYME *A × 4 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.4;20% (W/V) POLYETHYLENE GLYCOL (PEG) 3350, 0.1 M BIS-TRIS PROPANE PH 7.4, 0.2 M POTASSIUM THIOCYANATE
Resolution 2.10 Å R-free 0.237
5LS7 Complex of wild type E. coli alpha aspartate decarboxylase with its processing factor PanZ Deposited 2016-08-22 Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain B 1–127(127 aa)
Not recorded GOL GLYCEROL × 8 PEG DI(HYDROXYETHYL)ETHER × 8 ACO ACETYL COENZYME *A × 4 MG MAGNESIUM ION × 4 CO2 CARBON DIOXIDE × 12 SCN THIOCYANATE ION × 8 74C methyl radical × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.5;291 K;200 mM KSCN, 100 mM Bis-Tris propane pH 6.5, 20% v/v PEG 3350
Resolution 1.16 Å R-free 0.137