Current Protein Identity:P46275
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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 |