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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q51451 New Search
5PDB entries
8Biological assembly
10chain/assembly records
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
1HE1 Crystal structure of the complex between the GAP domain of the Pseudomonas aeruginosa ExoS toxin and human Rac Deposited 2000-11-18 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 95–229（135 aa） Fragment：96-234, GTPASE-ACTIVATING PROTEIN (GAP-DOMAIN)
Not recorded NI NICKEL (II) ION × 3 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；8% PEG 6000, 3MM NICL2, 100 MM TRIS/HCL PH8.5, pH 8.50
Resolution 2.00 Å R-free 0.224
1HE1 Crystal structure of the complex between the GAP domain of the Pseudomonas aeruginosa ExoS toxin and human Rac Deposited 2000-11-18 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 95–229（135 aa） Fragment：96-234, GTPASE-ACTIVATING PROTEIN (GAP-DOMAIN)
Not recorded NI NICKEL (II) ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 AF3 ALUMINUM FLUORIDE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；8% PEG 6000, 3MM NICL2, 100 MM TRIS/HCL PH8.5, pH 8.50
Resolution 2.00 Å R-free 0.224
1HE9 Crystal structure of the GAP domain of the Pseudomonas aeruginosa ExoS toxin Deposited 2000-11-21 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 102–235（134 aa） Fragment：96-234 GTPASE-ACTIVATING PROTEIN (GAP-DOMAIN)
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.5；MGCL2, (NH4)2SO4, PEG 6000, NA-CACODYLATE PH5.5, pH 5.50
Resolution 2.40 Å R-free 0.265
2C23 14-3-3 Protein Beta (Human) in complex with exoenzyme S peptide Deposited 2005-09-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain P 421–431（11 aa） Fragment：14-3-3 BINDING REGION, RESIDUES 421-431
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；0.05M MGCL2,0.1M HEPES PH7.5, 30% PEG MME 550, pH 8.00
Resolution 2.65 Å R-free 0.286
6GN0 Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form Deposited 2018-05-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain E 234–453（220 aa）
Chain G 234–453（220 aa）
Mutation：E379A, E381A Mutation：E379A, E381A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；12% PEG 3350, 4% Tacsimate
Resolution 3.24 Å R-free 0.294
6GN0 Exoenzyme S from Pseudomonas aeruginosa in complex with human 14-3-3 protein beta, tetrameric crystal form Deposited 2018-05-29 Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain F 234–453（220 aa）
Chain H 234–453（220 aa）
Mutation：E379A, E381A Mutation：E379A, E381A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5；277 K；12% PEG 3350, 4% Tacsimate
Resolution 3.24 Å R-free 0.294
6Y7T Engineered conjugation of lysine-specific molecular tweezers with ExoS derived peptidic inhibitor enhance affinity towards target protein 14-3-3 through ditopic binding Deposited 2020-03-02 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: TRIMERIC（3） Consistent with protein count
Chain D 420–430（11 aa）
Not recorded NA SODIUM ION × 3 GOL GLYCEROL × 1 TWZ 2-[4-[2-[hydroxy-[[(1R,5S,9S,16R,20R,24S,28S,35R)-22-phosphonooxy-3-tridecacyclo[22.14.1.15,20.19,16.128,35.02,23.04,21.06,19.08,17.010,15.025,38.027,36.029,34]dotetraconta-2,4(21),6(19),7,10,12,14,17,22,25(38),26,29,31,33,36-pentadecaenyl]oxy]phosphoryl]oxyethyl]triazol-1-yl]acetic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Bis-Tris Propane 0.2M sodium acetate trihydrate 20% PEG1000 10% Glycerol pH 7 Grew at 4 degree Celsius after a few days
Resolution 2.50 Å R-free 0.268
6Y7T Engineered conjugation of lysine-specific molecular tweezers with ExoS derived peptidic inhibitor enhance affinity towards target protein 14-3-3 through ditopic binding Deposited 2020-03-02 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: TRIMERIC（3） Consistent with protein count
Chain E 420–430（11 aa）
Not recorded NA SODIUM ION × 2 GOL GLYCEROL × 1 TWZ 2-[4-[2-[hydroxy-[[(1R,5S,9S,16R,20R,24S,28S,35R)-22-phosphonooxy-3-tridecacyclo[22.14.1.15,20.19,16.128,35.02,23.04,21.06,19.08,17.010,15.025,38.027,36.029,34]dotetraconta-2,4(21),6(19),7,10,12,14,17,22,25(38),26,29,31,33,36-pentadecaenyl]oxy]phosphoryl]oxyethyl]triazol-1-yl]acetic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；Bis-Tris Propane 0.2M sodium acetate trihydrate 20% PEG1000 10% Glycerol pH 7 Grew at 4 degree Celsius after a few days
Resolution 2.50 Å R-free 0.268

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.