Current Protein Identity：P07953
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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 |
|---|---|---|---|---|---|---|---|
| 1C7Z REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE Deposited 2000-04-03 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
251–440（190 aa）
Chain B
251–440（190 aa）
|
Not recorded | PO4 PHOSPHATE ION × 2 G3H GLYCERALDEHYDE-3-PHOSPHATE × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
EVAPORATION；pH 7.25；293 K；PEG 4000, sodium chloride, Hepes, pH 7.25, EVAPORATION, temperature 293.0K
|
Resolution 2.60 Å R-free 0.253 |
| 1C80 REGULATORY COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE Deposited 2000-04-03 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
251–440（190 aa）
Chain B
251–440（190 aa）
|
Not recorded | PO4 PHOSPHATE ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
EVAPORATION；pH 7.25；293 K；PEG 4000, sodium chloride, Hepes, pH 7.25, EVAPORATION, temperature 293.0K
|
Resolution 2.20 Å R-free 0.265 |
| 1C81 MICHAELIS COMPLEX OF FRUCTOSE-2,6-BISPHOSPHATASE Deposited 2000-04-03 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
251–440（190 aa）
|
Not recorded | FDQ 2,5-anhydro-1-deoxy-1-phosphono-6-O-phosphono-D-glucitol × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
EVAPORATION；pH 7.25；293 K；PEG 4000, sodium chloride, Hepes, pH 7.25, EVAPORATION, temperature 293.0K
|
Resolution 2.50 Å R-free 0.287 |
| 1FBT THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE Deposited 1996-03-08 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
251–440（190 aa）
Chain B
251–440（190 aa）
|
Mutation：30 AMINO ACIDS DELETED FROM THE C-TERMINAL Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：30 AMINO ACIDS DELETED FROM THE C-TERMINAL Non-standard monomer：Yes (specific site not provided by mmCIF) | PO4 PHOSPHATE ION × 2 | X-RAY DIFFRACTION | mmCIF provides none of the parsed conditions | Resolution 2.00 Å R-free 0.278 |
| 1TIP THE BISPHOSPHATASE DOMAIN OF THE BIFUNCTIONAL RAT LIVER 6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE Deposited 1997-05-28 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
251–440（190 aa）
Chain B
251–440（190 aa）
|
Mutation：30 C-TERMINAL AMINO ACIDS DELETED Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：30 C-TERMINAL AMINO ACIDS DELETED Non-standard monomer：Yes (specific site not provided by mmCIF) | F6P 6-O-phosphono-beta-D-fructofuranose × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
A CATALYTIC PHOSPHOSENZYME INTERMEDIATE STATE OF THE
BISPHOSPHATASE WAS PREPARED BY SOAKING OF THE NATIVE
CRYSTAL OF THE PROTEIN AND TRAPPED USING THE CRYOGENIC
DEVICE. A 2.2 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE
INTERMEDIATE WAS DETERMINED. A PHOSPHORYLATED CATALYTIC
HISTIDINE WAS VISUALIZED ALONG WITH THE FIRST PRODUCT,
FRUCTOSE-6 - PHOSPHATE, AND THE CATALYTIC WATER, SHOWING
THE COMPREHENSIVE GEOMETRY OF A TRIGONAL BI-PYRAMIDAL
STRUCTURE.
|
Resolution 2.20 Å R-free 0.286 |