Current Protein Identity:P00586 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification 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
1BOH SULFUR-SUBSTITUTED RHODANESE (ORTHORHOMBIC FORM) Deposited 1998-08-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–296(296 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.3;pH 7.3
Resolution 2.30 Å R-free 0.215
1BOI N-TERMINALLY TRUNCATED RHODANESE Deposited 1998-08-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–296(296 aa) Fragment:DEL(1-7)
Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.3;pH 7.3
Resolution 2.20 Å R-free 0.219
1DP2 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RHODANESE AND LIPOATE Deposited 1999-12-23 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–293(293 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) LPB 5-[(3S)-1,2-dithiolan-3-yl]pentanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;Crystals were obtained from ammonium sulfate. After soaking with 28% PEG 6000, 40 mM phosphate buffer, pH=7, 4 mM DL-lipoate was added , VAPOR DIFFUSION, SITTING DROP, temperature 20K, temperature 293K
Resolution 2.01 Å R-free 0.230
1ORB ACTIVE SITE STRUCTURAL FEATURES FOR CHEMICALLY MODIFIED FORMS OF RHODANESE Deposited 1995-07-24 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–296(296 aa)
Not recorded ACT ACETATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å
1RHD STRUCTURE OF BOVINE LIVER RHODANESE. I. STRUCTURE DETERMINATION AT 2.5 ANGSTROMS RESOLUTION AND A COMPARISON OF THE CONFORMATION AND SEQUENCE OF ITS TWO DOMAINS Deposited 1977-11-23 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–293(293 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å
1RHS SULFUR-SUBSTITUTED RHODANESE Deposited 1997-07-16 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–296(296 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.6;pH 7.6
Resolution 1.36 Å R-free 0.229
2ORA RHODANESE (THIOSULFATE: CYANIDE SULFURTRANSFERASE) Deposited 1996-02-22 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–296(296 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.99 Å
8Q5Z Crystal structure of bovine Thiosulfate sulfurtransferase Deposited 2023-08-10 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 1–297(297 aa)
Not recorded NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;291 K;PEG 6000, Tris, calcium chloride dihydrate
Resolution 1.50 Å R-free 0.163