Current Protein Identity:Q980E5 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
3TCO Crystallographic and spectroscopic characterization of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability Deposited 2011-08-09 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 25–133(109 aa) Fragment:Truncated form (25-133) of Thioredoxin (TrxA-1)
Not recorded EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;30% (w/v) PEG4000; 0.2 M Ammonium sulfate. Protein concentration 2-6 mg/ml., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.222
3TCO Crystallographic and spectroscopic characterization of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability Deposited 2011-08-09 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 25–133(109 aa) Fragment:Truncated form (25-133) of Thioredoxin (TrxA-1)
Not recorded EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;30% (w/v) PEG4000; 0.2 M Ammonium sulfate. Protein concentration 2-6 mg/ml., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.222
3TCO Crystallographic and spectroscopic characterization of Sulfolobus solfataricus TrxA1 provide insights into the determinants of thioredoxin fold stability Deposited 2011-08-09 Assembly 3 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain C 25–133(109 aa) Fragment:Truncated form (25-133) of Thioredoxin (TrxA-1)
Not recorded EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 6.5;293 K;30% (w/v) PEG4000; 0.2 M Ammonium sulfate. Protein concentration 2-6 mg/ml., pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.222
6H1Y CRYSTAL STRUCTURE OF A CHIMERIC VARIANT OF THIOREDOXIN FROM ESCHERICHIA COLI Deposited 2018-07-12 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 40–47(8 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;Crystals were obtained with a protein concentration of 20-25 mg/ml. The composition of the reservoir solution was 17% (w/v) PEG10000, 0.1 M ammonium acetate and 0.1 M BIS-TRIS buffer, pH 5.5.
Resolution 2.99 Å R-free 0.259
6H1Y CRYSTAL STRUCTURE OF A CHIMERIC VARIANT OF THIOREDOXIN FROM ESCHERICHIA COLI Deposited 2018-07-12 Assembly 2 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 40–47(8 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;Crystals were obtained with a protein concentration of 20-25 mg/ml. The composition of the reservoir solution was 17% (w/v) PEG10000, 0.1 M ammonium acetate and 0.1 M BIS-TRIS buffer, pH 5.5.
Resolution 2.99 Å R-free 0.259