Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
dimer or tetramer
x * 25000, recombinant enzyme, SDS-PAGE
monomer or dimer
O15217, O43708, O60760, P08263, P09210, P09211, P09488, P0CG30, P21266, P28161, P46439, P78417, Q03013, Q16772, Q7RTV2, Q9H4Y5 the class GST occurs in a monomer-dimer equilibrium
?
x * 25000, SDS-PAGE
?
-
x * 25348-25528, alpha class isozyme, mass spectrometry, x * 23548, pi class isozyme, MALDI-TOF mass spectrometry, x * 26027, mu class isozyme, MALDI-TOF mass spectrometry
?
x * 24000, isozyme GST-1, SDS-PAGE
?
-
x * 26560, calculated from amino acid sequence
?
-
x * 25000, isozyme GSTF9, SDS-PAGE
?
-
x * 28000, isozyme GSTU26, SDS-PAGE
?
-
x * 23500, MALDI mass spectrometry
?
-
x * 23500, MALDI mass spectrometry
-
?
-
x * 67000, SDS-PAGE. Enzyme isoforms are located in the region corresponding to the marker protein with a molecular mass of 67000 Da or a little below
?
x * 23338, GSTO, sequence calculation
?
x * 24225, GSTO, sequence calculation
?
x * 29806, GSTO, sequence calculation
?
-
x * about 26000, SDS-PAGE
?
-
x * 24190, calculated from amino acid sequence
?
x * 23530, calculated from amino acid sequence
?
-
x * 25705, isozyme Der p 8, sequence calcualtion
?
x * 148060, calculated from amino acid sequence
?
x * 80400, calculated from amino acid sequence
?
x * 97700, calculated from amino acid sequence
?
-
x * 25000, recombinant enzyme, SDS-PAGE
?
-
x * 27400, HdGSTO1, sequence calculation, x * 26900, HdGSTO2, sequence calculation
?
x * 25740, isoform GSTmu, calculated from amino acid sequence
?
x * 26060, isoform GSTrho, calculated from amino acid sequence
?
x * 68240, recombinant isoform GSTmu bound to maltose-binding protein, SDS-PAGE
?
x * 68590, recombinant isoform GSTrho bound to maltose-binding protein, SDS-PAGE
?
-
x * 24300, recombinant His6-tagged wild-type GSTZ1-1, SDS-PAGE
?
x * 23204, sequence calculation
?
x * 23300, calculated from amino acid sequence
?
-
x * 25000, SDS-PAGE
-
?
x * about 45000, SDS-PAGE
?
-
x * about 45000, SDS-PAGE
-
?
x * 24000-26000, liver enzyme, SDS-PAGE
?
x * 25180, GSTU17, sequence calculation
?
x * 26938, isoform GSTO7, calculated from amino acid sequence
?
x * 26938, native isoform GSTO7, mass spectrometry
?
x * 27713, isoform GSTO4, calculated from amino acid sequence
?
x * 30019, native isoform GSTO4, mass spectrometry
?
x * 27370, His6-tagged recombinant enzyme, calculated from amino acid sequence
?
x * 25378, isoform GSTU45, calculated from amino acid sequence
?
x * 25521, isoform GSTU16, calculated from amino acid sequence
?
x * about 30000, SDS-PAGE
?
-
x * 30400, calculated from amino acid sequence
?
-
x * 35100, recombinant enzyme, SDS-PAGE
?
-
x * 30400, calculated from amino acid sequence
-
?
-
x * 35100, recombinant enzyme, SDS-PAGE
-
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 26100, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 24756, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 24893, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25014, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25172, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25262, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25300, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25340, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25401, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25493, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25536, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25567, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 25680, calculated from amino acid sequence
?
A0A4Y5QZW9, A0A4Y5QZX0, A0A4Y5QZX2, A0A4Y5QZX3, A0A4Y5QZX9, A0A4Y5QZZ8, A0A4Y5R032, A0A4Y5R087, A0A4Y5R0B2, A0A4Y5R0C1, A0A4Y5R0K8, A0A4Y5R0L5, A0A4Y5R2M7, A0A4Y5R2N2 x * 26434, calculated from amino acid sequence
?
-
x * 23600, calculated from amino acid sequence
?
-
x * 22281, isoform GST20, calculated from amino acid sequence
?
-
x * 25942, isoform GST7, calculated from amino acid sequence
?
-
x * 25280, calculated from amino acid sequence
?
-
x * 24490, calculated from amino acid sequence
dimer
-
1 * 29000 + 1 * 25000, SDS-PAGE
dimer
-
2 * 25000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
dimer
-
2 * 27000, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE
dimer
2 * 22000, SDS-PAGE
dimer
-
subunit dimerization is mainly formed by an electrostatic interaction and a distinctive lock-and-key clasp motif for Delta class GSTs, GSTD1 and GSTD10 structure, modeling, GST tertiary structures comparisons, overview
dimer
-
2 * 25600, recombinant cytosolic isozyme, SDS-PAGE
dimer
-
2 * 22500 (about)
dimer
-
2 * 22500 (about)
-
dimer
-
2 * 22500 (about)
dimer
-
2 * 23000, SDS-PAGE
dimer
-
2 * 24000, GSH-S transferase rho, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
subunit-subunit interactions of isozyme GST Nu2-2, crystal structure analysis, overview
dimer
O15217, O43708, O60760, P08263, P09210, P09211, P09488, P0CG30, P21266, P28161, P46439, P78417, Q03013, Q16772, Q7RTV2, Q9H4Y5 -
dimer
-
crystal structure
dimer
-
2 * 22000, SDS-PAGE
dimer
-
dimeric forms: B1B1, B2B2 and B1B2
dimer
-
2 * 25600, form XIII, SDS-PAGE
dimer
-
2 * 25200, form I-XII, SDS-PAGE
dimer
-
2 * 23000, acidic isoenzyme, SDS-PAGE
dimer
-
2 * 25000, basic isoenzyme, SDS-PAGE
dimer
-
homodimer, C-terminal region structure of isozyme GST-A1-1, which can adopt an ordered helix-like structure even in the apo state, but shows a strong tendency to unwind, overview
dimer
2 * 26700, isozyme SIGST, SDS-PAGE
dimer
-
2 * 22500 (about)
dimer
-
2 * 23000, SDS-PAGE
dimer
-
1 * 23310 + 1 * 20430, enzyme of Nanyang city population, SDS-PAGE, 1 * 53140 + 1 * 20130, enzyme of Wuzhou population, SDS-PAGE, 1 * 50790 + 1 * 19420, enzyme of Hezhou population, SDS-PAGE
dimer
-
2 * 24000, SDS-PAGE
dimer
-
2 * 24100, SDS-PAGE
dimer
-
pi and theta class enzymes are homodimers, alpha and mu class enzymes can be homo- or heterodimeric
dimer
-
2 * 23400, SDS-PAGE
dimer
-
2 * 23000, enzyme MII, SDS-PAGE
dimer
-
2 * 25000, enzyme MI, SDS-PAGE
dimer
-
2 * 26500, enzyme MIII, SDS-PAGE
dimer
-
2 * 30000, GST I, SDS-PAGE
dimer
-
1 * 25000 + 1 * 28000, GST II-III, SDS-PAGE
dimer
-
2 * 26000, anionic isoenzyme
dimer
-
2 * 24000, cationic isoenzyme
dimer
2 * 28000, enzyme form GSTR1, SDS-PAGE
dimer
-
2 * 25000, SDS-PAGE
dimer
2 * 25452, recombinant isozyme GSTT1, mass spectrometry and SDS-PAGE
dimer
2 * 31800, SDS-PAGE
dimer
-
1 * 30000 + 1 * 27500 or 1 * 30000 + 1 * 29000, SDS-PAGE, GSTF
dimer
-
1 * 27500 + 1 * 29000, SDS-PAGE, GSTC and GPOX
dimer
-
active enzyme form, in the presence of 2 mM glutathione
dimer
2 * 25000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 22500 (about)
dimer
-
2 * 22500 (about)
-
dimer
-
2 * 22500 (about)
dimer
-
2 * 22500 (about)
-
dimer
-
2 * 22500 (about)
dimer
-
2 * 23500, SDS-PAGE
dimer
-
2 * 26000, SDS-PAGE
dimer
-
2 * 24400, SDS-PAGE
dimer
-
dimer composed of two of the following subunits: Ya MW 23000, Yb MW 23500, Yc MW 25000, SDS-PAGE
dimer
-
wild-type isozyme GST-M1-1, homodimer, crystal structure determination
dimer
2 * 26000, gel filtration
dimer
-
2 * 22500 (about)
dimer
-
2 * 22500 (about)
-
dimer
-
2 * 22000, SDS-PAGE
dimer
-
2 * 26000, isoenzyme VII, SDS-PAGE
dimer
-
1 * 27100 + 1 * 28700, isoenzyme I, SDS-PAGE
dimer
-
2 * 26400, isoenzyme VI, SDS-PAGE
dimer
-
1 * 27100 + 1 * 26800, isoenzyme IV, SDS-PAGE
dimer
2 * 27328, electrospray ionization MS
dimer
-
1 * 26800 + 1 * 26000, isoenzyme V, SDS-PAGE
dimer
-
2 * 26500, SDS-PAGE
dimer
-
1 * 32600 + 1 * 36800, enzyme occurs as homodimeric form and as heterodimeric form, SDS-PAGE
dimer
-
2 * 34000, enzyme occurs as homodimeric form and as heterodimeric form, SDS-PAGE
dimer
-
2 * 24500, SDS-PAGE
dimer
-
2 * 22800 or 2 * 24600, SDS-PAGE
dimer
-
2 * 29000, enzyme GST II, SDS-PAGE
dimer
-
2 * 29000, enzyme GST I, SDS-PAGE
heterodimer
-
-
heterodimer
-
1 * 27500 + 1 * 26000, gel filtration
heterodimer
-
1 * 28000 + 1 * 27200, gel filtration
heterodimer
-
1 * 29000 + 1 * 28000, gel filtration
heterodimer
-
1 * 30000 + 1 * 27500, gel filtration
heterodimer
Q2G4B4; Q2G4B5
1 * 29400 + 1 * 27000, SDS-PAGE
heterodimer
-
1 * 29400 + 1 * 27000, SDS-PAGE
-
homodimer
2 * 30000
homodimer
-
2 * 27000, SDS-PAGE
homodimer
2 * 25100, gel filtration
homodimer
2 * 30000, SDS-PAGE
homodimer
2 * 25000, SDS-PAGE
homodimer
2 * 28700, isoform GstO2B, calculated from amino acid sequence
homodimer
2 * 29100, isoform GstO2A, calculated from amino acid sequence
homodimer
2 * 24535, calculated from amino acid sequence
homodimer
-
2 * 25000, SDS-PAGE
homodimer
2 * 25000, SDS-PAGE
homodimer
2 * 31000, SDS-PAGE
homodimer
2 * 29830, calculated from amino acid sequence
homodimer
-
x-ray crystallography
homodimer
2 * 23000, X-ray crystallography
homodimer
-
2 * 26000, SDS-PAGE
homodimer
-
2 * 25900, MALDI-TOF mass spectrometry
homodimer
x-ray crystallography
homodimer
the GST5118 monomer adopts the GST canonical fold, which consists of an N-terminal thioredoxin-like motif and a C-terminal domain of at least four helices, unique dimeric organization of GST5118, overview
homodimer
Q8MU52
2 * 25000
homodimer
-
2 * 24600, MALDI-TOF spectrometry
homodimer
-
2 * 26800, isoform GST2, SDS-PAGE
homodimer
-
2 * 27500, isoform GST1, SDS-PAGE
homodimer
2 * 26500, gel filtration
homodimer
2 * 28000, in solution, gel filtration
monomer
-
-
monomer
-
x-ray crystallography
monomer
-
mutant isozyme GST-M1, crystal structure determination
tetramer
-
a tetramer that dissociates into dimers in the presence of glutathione
tetramer
-
4 * 26000, gel filtration, inactive enzyme form under native conditions
trimer
-
structure of TDR1 reveals a unique trimer of subunits each containing two glutathione-S-transferase domains. The TDR1 subunit is constructed from two GST-like domains with a short linker region. The domains themselves consist of N-terminal glutaredoxin-like and C-terminal alpha-helical subdomains
trimer
-
native MGST1 binds three GSH molecules per trimer but with different affinities for GSH, it possesses only one high affinity catalytically competent site per trimer, nanoelectrospray mass spectrometric analysis, overview
additional information
-
isozymes identification by nanospray liquid chromatographytandem mass spectrometry, peptide mass mapping, and MS/MS sequencing, overview
additional information
-
structural model of the wild-type GST adgstD4-4 shows that Val107 is located in the subunit-interface region of the dimeric GST, forming part of an intersubunit lock-and key clasp motif
additional information
the aromatic zipper motif contributes to modulating the protein structure, which impacts on protein stability and the topological arrangement of the active site
additional information
agGSTe2 is a canonical GST fold with a highly conserved N-domain and a less conserved C-domain, isozyme agGSTe2 amino acid sequence and secondary structure comparisons, overview
additional information
-
agGSTe2 is a canonical GST fold with a highly conserved N-domain and a less conserved C-domain, isozyme agGSTe2 amino acid sequence and secondary structure comparisons, overview
additional information
-
molecular modeling of the GSTZ substrate superimposed enzyme using the apoform crystal structure of AtGSTZ monomer
additional information
-
bmGSTD contains two distinct domains, an N-terminal domain and a C-terminal domain, connected by a linker. The N-terminal domain binds glutathione
additional information
secondary structure of GmGSTU4-4 from PDB ID 2VO4 and sequence comparisons, overview
additional information
-
secondary structure of GmGSTU4-4 from PDB ID 2VO4 and sequence comparisons, overview
additional information
-
three-dimensional structure determination of HdGSTO1 and HdGSTO2 by homology modeling, overview
additional information
-
quantitative structure-activity relationship analyses, calculation, overview
additional information
-
structure-activity relationships, overview
additional information
the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview
additional information
-
the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview
additional information
-
wild-type hGSTZ1-1 and mutant seleno-hGSTZ1-1 three-dimensional structure modeling, overview
additional information
peptide mapping of Sigma and Delta class isozymes using the sequences of GSTs from Drosophila melanogaster and Musca domestica, overview
additional information
-
peptide mapping of Sigma and Delta class isozymes using the sequences of GSTs from Drosophila melanogaster and Musca domestica, overview
additional information
-
trichinellosis and of albendazole treatment influence the quaternary structure of cytosolic GST in muscles during experimental trichinellosis in mice, overview
additional information
-
the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview
additional information
-
trichinellosis and of albendazole treatment influence the quaternary structure of cytosolic GST in muscles during experimental trichinellosis in mice, overview
-
additional information
isozyme MdGST6B shows typical GST folding comprised of N-terminal and C-terminal domains
additional information
-
isozyme MdGST6B shows typical GST folding comprised of N-terminal and C-terminal domains
additional information
isozyme identification by Fourier transform-ion cyclotron resonance mass spectrometer analysis, overview
additional information
isozyme identification by Fourier transform-ion cyclotron resonance mass spectrometer analysis, overview
additional information
-
isozyme identification by Fourier transform-ion cyclotron resonance mass spectrometer analysis, overview
additional information
-
isozyme identification by nanospray liquid chromatography-tandem mass spectrometry, peptide sequence determination
additional information
structure homology modeling
additional information
-
structure homology modeling
additional information
-
tertiary and quaternary structure of the enzyme with bound S-hexylglutathione
additional information
unfolding behavior of Plasmodium vivax GST is significantly different from Plasmodium falciparum GST, the unfolding pathway of Plasmodium vivax GST is non-cooperative with stabilization of an inactive dimeric intermediate. The absence of any compact folded monomeric intermediate during the unfolding transition suggests that inter-subunit interactions play an important role in stabilizing the protein, overview. Three-dimensional modeling, overview
additional information
-
unfolding behavior of Plasmodium vivax GST is significantly different from Plasmodium falciparum GST, the unfolding pathway of Plasmodium vivax GST is non-cooperative with stabilization of an inactive dimeric intermediate. The absence of any compact folded monomeric intermediate during the unfolding transition suggests that inter-subunit interactions play an important role in stabilizing the protein, overview. Three-dimensional modeling, overview
additional information
-
more than one subunit
additional information
-
homology modeling of recombinant isozyme GSTA1-1 with and without bound inhibitor 2,3,5,6-tetrachloro-1,4-benzoquinone
additional information
-
molecular structure modeling, the wild-type dimeric form is not required for catalytic activity, overview
additional information
-
quantitative structure-activity relationship analyses, calculation, overview
additional information
-
the substrate recognition H-site is formed by several segments of amino acid residues located in separate regions of the primary structure. The C-terminal helix of the protein serves as a lid over the active site, and contributes several residues to the H-site, molecular modeling, overview
additional information
structure analysis shows flexibility of the substrate-binding site
additional information
-
structure analysis shows flexibility of the substrate-binding site
additional information
-
structure-function study of glutathione transferase-like proteins, Structure-based multiple sequence alignments, overview