Current Protein Identity:Q47898 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state 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
1AYY GLYCOSYLASPARAGINASE Deposited 1997-11-12 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 46–196(151 aa)
Chain B 197–340(144 aa)
Chain C 46–196(151 aa)
Chain D 197–340(144 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5;19% PEG3350 IN 100 MM TRIS.HCL PH 8.5
Resolution 2.32 Å R-free 0.270
1P4K CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT Deposited 2003-04-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 46–340(295 aa) Fragment:Glycosylasparaginase, alpha and beta chains
Chain C 46–340(295 aa) Fragment:Glycosylasparaginase, alpha and beta chains
Mutation:D151N Mutation:D151N GOL GLYCEROL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;pH 7.5;15% PEG 3300, 0.1M Tris, pH 7.5, 0.2M lithium sulfate, 0.1% sodium azide, EVAPORATION
Resolution 1.90 Å R-free 0.220
1P4V CRYSTAL STRUCTURE OF THE GLYCOSYLASPARAGINASE PRECURSOR D151N MUTANT WITH GLYCINE Deposited 2003-04-24 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 46–340(295 aa) Fragment:Glycosylasparaginase, alpha and beta chains
Chain C 46–340(295 aa) Fragment:Glycosylasparaginase, alpha and beta chains
Mutation:D151N Mutation:D151N GLY GLYCINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION;pH 7.5;15% PEG 3300, 0.1M Tris, pH 7.5, 0.2M lithium sulfate, 0.1% sodium azide, 0.05M glycine, EVAPORATION
Resolution 1.90 Å R-free 0.225
2GAC T152C MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM Deposited 1998-05-29 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 46–196(151 aa)
Chain B 198–340(143 aa)
Chain C 46–196(151 aa)
Chain D 198–340(143 aa)
Mutation:T152C Mutation:T152C Mutation:T152C Mutation:T152C No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;pH 7.5
Resolution 2.10 Å R-free 0.280
2GAW WILD TYPE GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM Deposited 1998-05-29 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 46–196(151 aa)
Chain B 197–340(144 aa)
Chain C 46–196(151 aa)
Chain D 197–340(144 aa)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;pH 7.5
Resolution 2.20 Å R-free 0.297
2GL9 Crystal Structure of Glycosylasparaginase-Substrate Complex Deposited 2006-04-04 Assembly 1 Protein homooligomer Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 46–196(151 aa) Fragment:residues 46-196
Chain B 197–340(144 aa) Fragment:residues 197-340
Chain C 46–196(151 aa) Fragment:residues 46-196
Chain D 197–340(144 aa) Fragment:residues 197-340
Mutation:T152C Mutation:T152C NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ASN ASPARAGINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;298 K;15% PEG 3350, 100 mM HEPES, 0.1% sodium azide, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.00 Å R-free 0.215
3LJQ Crystal Structure of the Glycosylasparaginase T152C apo-precursor Deposited 2010-01-26 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 46–340(295 aa) Fragment:UNP residues 46-340
Chain C 46–340(295 aa) Fragment:UNP residues 46-340
Mutation:T152C Mutation:T152C NA SODIUM ION × 2 GLY GLYCINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;277 K;15% PEG 3350, 100 mM HEPES pH 7.5, 0.1% sodium azide, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.90 Å R-free 0.197
4R4Y Structural basis of a point mutation that causes the genetic disease Aspartylglucosaminuria Deposited 2014-08-20 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 46–340(295 aa) Fragment:UNP residues 46-340
Chain B 46–340(295 aa) Fragment:UNP residues 46-340
Mutation:G172D Mutation:G172D SD4 N-hydroxy-L-asparagine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5;298 K;0.2M NaCl, 0.1M Bis-Tris pH 6.5, 25% PEG 3350., VAPOR DIFFUSION, SITTING DROP, temperature 298.0K
Resolution 2.10 Å R-free 0.252
9GAA PRECURSOR OF THE T152A MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM Deposited 1999-06-15 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 46–340(295 aa)
Mutation:T152A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;PROTEIN WAS CRYSTALLIZED FROM 15% PEG 3300, 100MM TRIS, PH 7.5, 0.2M LITHIUM SULFATE, 0.1% SODIUM AZIDE
Resolution 2.10 Å R-free 0.297
9GAA PRECURSOR OF THE T152A MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM Deposited 1999-06-15 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain C 46–340(295 aa)
Mutation:T152A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;PROTEIN WAS CRYSTALLIZED FROM 15% PEG 3300, 100MM TRIS, PH 7.5, 0.2M LITHIUM SULFATE, 0.1% SODIUM AZIDE
Resolution 2.10 Å R-free 0.297
9GAA PRECURSOR OF THE T152A MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM Deposited 1999-06-15 Assembly 3 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 46–340(295 aa)
Chain C 46–340(295 aa)
Mutation:T152A Mutation:T152A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;PROTEIN WAS CRYSTALLIZED FROM 15% PEG 3300, 100MM TRIS, PH 7.5, 0.2M LITHIUM SULFATE, 0.1% SODIUM AZIDE
Resolution 2.10 Å R-free 0.297
9GAC PRECURSOR OF THE T152C MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM Deposited 1999-06-15 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 46–340(295 aa)
Chain C 46–340(295 aa)
Mutation:T152C Mutation:T152C GLY GLYCINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;PROTEIN WAS CRYSTALLIZED FROM 15% PEG 3300, 100MM TRIS, PH 7.5, 0.2M LITHIUM SULFATE, 0.1% SODIUM AZIDE
Resolution 1.90 Å R-free 0.278
9GAF PRECURSOR OF THE W11F MUTANT GLYCOSYLASPARAGINASE FROM FLAVOBACTERIUM MENINGOSEPTICUM Deposited 1999-06-15 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 47–340(294 aa)
Chain C 47–340(294 aa)
Mutation:W11F Mutation:W11F GLY GLYCINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5;PROTEIN WAS CRYSTALLIZED FROM 15% PEG 3300, 100MM TRIS, PH 7.5, 0.2M LITHIUM SULFATE, 0.1% SODIUM AZIDE
Resolution 1.90 Å R-free 0.239