Current Protein Identity:P46275 New Search
Main Difference Dimensions in This Set
Different mutation/modification 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
1D9Q OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATASE FORM 1 Deposited 1999-10-29 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 51–407(357 aa)
Chain B 51–407(357 aa)
Chain C 51–407(357 aa)
Chain D 51–407(357 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5;290 K;25% PEG 400, 50MM NA ACETATE (PH 5.5), 50MM MGCL2, 5MM F6P, VAPOR DIFFUSION, HANGING DROP, temperature 290K
Resolution 2.40 Å R-free 0.236
1DBZ C153S MUTANT OF PEA FRUCTOSE-1,6-BISPHOSPHATASE Deposited 1999-11-03 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 51–407(357 aa)
Chain B 51–407(357 aa)
Chain C 51–407(357 aa)
Chain D 51–407(357 aa)
Mutation:C153S Mutation:C153S Mutation:C153S Mutation:C153S No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5;291 K;20% PEG 1000, 50MM NA ACETATE (PH 5), 50 MM MGCL2, 5MM F6P, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.65 Å R-free 0.291
1DCU REDOX SIGNALING IN THE CHLOROPLAST: STRUCTURE OF OXIDIZED PEA FRUCTOSE-1,6-BISPHOSPHATE PHOSPHATASE Deposited 1999-11-05 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 51–407(357 aa)
Chain B 51–407(357 aa)
Chain C 51–407(357 aa)
Chain D 51–407(357 aa)
Mutation:A197I, E232K Mutation:A197I, E232K Mutation:A197I, E232K Mutation:A197I, E232K No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;PEG 400, Na acetate, magnesium chloride, fructose-6-phosphate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K
Resolution 2.20 Å R-free 0.247