Current Protein Identity：P00963
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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 |
|---|---|---|---|---|---|---|---|
| 11AS ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE Deposited 1997-12-02 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
1–330（330 aa）
Chain B
1–330（330 aa）
|
Mutation：C51A, C315A Mutation：C51A, C315A | ASN ASPARAGINE × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 7.5；PROTEIN CRYSTALLIZED FROM 45% SATURATED AMMONIUM SULFATE, 22 MM ASPARAGINE, 88 MM MGCL2, 10 %(W/V) GLYCEROL 5 MM 2-MERCAPTOETHANOL, 50 MM HEPES, PH7.5
|
Resolution 2.50 Å R-free 0.253 |
| 12AS ASPARAGINE SYNTHETASE MUTANT C51A, C315A COMPLEXED WITH L-ASPARAGINE AND AMP Deposited 1997-12-02 | Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count |
Chain A
1–330（330 aa）
Chain B
1–330（330 aa）
|
Mutation：C51A, C315A Mutation：C51A, C315A | ASN ASPARAGINE × 2 AMP ADENOSINE MONOPHOSPHATE × 2 | X-RAY DIFFRACTION |
X-ray crystallization conditions
pH 7.5；PROTEIN CRYSTALLIZED FROM 45% SATURATED AMMONIUM SULFATE, 22 MM ASPARAGINE, 88 MM MGCL2, 10 %(W/V) GLYCEROL 5 MM 2-MERCAPTOETHANOL, 50 MM HEPES, PH7.5 THEN SOAKED BY 50MM AMP AND 50 MM ASPARAGINE
|
Resolution 2.20 Å R-free 0.287 |