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trimer
-
and dimer, 3 * 86000, SDS-PAGE and chemical crosslinking, isoform ICD-2
?
x * 48000, SDS-PAGE
?
x * 46705 , sequence calculation
?
-
x * 46705 , sequence calculation
-
?
x * 45836, calculated from amino acid sequence
?
x * 65000, TRX-tagged enzyme, SDS-PAGE
?
-
x * 44000, SDS-PAGE
-
?
-
x * 45836, calculated from amino acid sequence
-
?
-
x * 65000, TRX-tagged enzyme, SDS-PAGE
-
?
Q8X277
x * 45837, sequence calculation, x * 60000, recombinant, renatured enzyme, SDS-PAGE
?
-
x * 48100, calculated from amino acid sequence
?
-
x * 45000, isozyme ICD1, SDS-PAGE
?
x * 47000, approximately, cytosolic and mitochondrial isozymes, SDS-PAGE
?
-
x * 46381, isozyme IDP1, mass spectrometry, x * 46562, isozyme IDP2, mass spectrometry, x * 47856, isozyme IDP3, mass spectrometry
?
-
x * 40000, SDS-PAGE
-
?
x * 45000, calculated from amino acid sequence
?
x * 45000, recombinant N-terminally His6-tagged enzyme, SDS-PAGE
dimer
dissociation from dimer to monomer at pH 3.0
dimer
-
dissociation from dimer to monomer at pH 3.0
-
dimer
alpha2, 2 * 42000, SDS-PAGE
dimer
-
alpha2, 2 * 45000, SDS-PAGE
dimer
-
alpha2, 2 * 48000, SDS-PAGE
dimer
-
alpha2, 2 * 40000, SDS-PAGE
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 62000, SDS-PAGE
dimer
Q8X277
the enzyme is a dimer at high salt concentration. Deactivation due to incubation of the enzyme at low NaCl concentrations is related to irreversible dissociation of the active dimeric species towards a monomer
dimer
-
2 * 62000, SDS-PAGE
-
dimer
-
2 * 49000, isoform ICD-1, 2 * 86000, isoform ICD-2, SDS-PAGE. Besides dimers, isoform ICD-1 forms some tetramer, ICD-2 forms trimer
dimer
isoform ICD1, X-ray crystallography
dimer
-
alpha2, 2 * 53000, SDS-PAGE
dimer
Pinus spp.
-
alpha2, 2 * 46000, SDS-PAGE
dimer
-
2 * 51000, about, recombinant enzyme, SDS-PAGE
dimer
2 * 45000, SDS-PAGE
dimer
-
2 * 45000, SDS-PAGE
-
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
-
dimer
2 * 47000, SDS-PAGE
dimer
2 * 43000, recombinant wild-type and mutant enzymes, SDS-PAGE
dimer
-
2 * 46600, recombinant thrombin cleaved wild-type and mutant enzymes, SDS-PAGE
dimer
-
residues Arg314, Tyr316, Lys321, and Arg323 are not involved in subunit interaction
dimer
-
wild-type and mutant enzymes, circular dichroism and native PAGE
dimer
-
alpha2, 2 * 57000, SDS-PAGE
dimer
-
alpha2, 2 * 30500, SDS-PAGE
dimer
-
alpha2, 2 * 30500, SDS-PAGE
-
dimer
and tetramer, crystallization data and analytical ultracentrifugation
dimer
2 * 45400, equilibrium of dimeric and tetrameric species, calculated from sequence
dimer
-
2 * 45400, equilibrium of dimeric and tetrameric species, calculated from sequence
-
homodimer
2 * 45000, SDS-PAGE
homodimer
2 * 83500, SDS-PAGE
homodimer
2 * 47900, calculated from sequence
homodimer
-
2 * 47900, calculated from sequence
-
homodimer
2 * 48300, His-tagged enzyme, calculated from amino acid sequence
homodimer
2 * 45000, recombinant His6-tagged enzyme, SDS-PAGE
homodimer
-
2 * 45000, recombinant His6-tagged enzyme, SDS-PAGE
-
homodimer
2 * 46200, estimated from amino acid sequence
homodimer
2 * 45000, SDS-PAGE
homodimer
2 * 44600, calculated from amino acid sequence
homodimer
-
2 * 45000, SDS-PAGE
-
homodimer
-
2 * 44600, calculated from amino acid sequence
-
homodimer
2 * 52600, SDS-PAGE
homodimer
each subunit has a Rossmann fold, and a common top domain of interlocking beta sheets
homodimer
-
each subunit has a Rossmann fold, and a common top domain of interlocking beta sheets
-
homodimer
2 * 45000, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 45000, recombinant enzyme, SDS-PAGE
-
monomer
dissociation from dimer to monomer at pH 3.0
monomer
-
dissociation from dimer to monomer at pH 3.0
-
monomer
-
1 * 80000, His-tagged enzyme, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
1 * 80000, SDS-PAGE
monomer
1 * 81000, calculated from amino acid sequence
monomer
-
1 * 80000, SDS-PAGE
-
monomer
-
1 * 81000, calculated from amino acid sequence
-
monomer
isoform ICD2, X-ray crystallography
monomer
-
1 * 80000, His-tagged enzyme, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 80426, calculated from amino acid sequence
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
-
monomer
1 * 72000, gel filtration
monomer
-
1 * 72000, gel filtration
-
monomer
-
1 * 80000, SDS-PAGE
monomer
-
1 * 80000, SDS-PAGE
-
monomer
-
isoenzyme II, 1 * 85000, SDS-PAGE
monomer
-
isoenzyme II, 1 * 85000, SDS-PAGE
-
monomer
-
1 * 80000, SDS-PAGE
tetramer
-
4 * 49000, isoform ICD-1, SDS-PAGE. Main form is dimer for isoform ICD-1
tetramer
and dimer, crystallization data and analytical ultracentrifugation
tetramer
4 * 45400, equilibrium of dimeric and tetrameric species, calculated from sequence
tetramer
-
4 * 45400, equilibrium of dimeric and tetrameric species, calculated from sequence
-
additional information
prediction and analysis of structures and conserved domains of pepper NADP-ICDH containing 172 alpha helices, 84 extended strands, 32 beta turn, and 127 random coils, homology modeling, overview
additional information
-
prediction and analysis of structures and conserved domains of pepper NADP-ICDH containing 172 alpha helices, 84 extended strands, 32 beta turn, and 127 random coils, homology modeling, overview
-
additional information
-
enzyme has 3 different conformational stages
additional information
exchange of Arg132 to His affects the conformation equilibrium and the reorganization of the active-site. Also, not only the expected loss of key salt-bridge interactions between the guanidinium of R132 and the alpha/beta carboxylates of isocitrate, as well as changes in the network that coordinates the metal ion, but also an unexpected reorganization of the active-site, structure analyis, overview
additional information
-
exchange of Arg132 to His affects the conformation equilibrium and the reorganization of the active-site. Also, not only the expected loss of key salt-bridge interactions between the guanidinium of R132 and the alpha/beta carboxylates of isocitrate, as well as changes in the network that coordinates the metal ion, but also an unexpected reorganization of the active-site, structure analyis, overview
additional information
three-dimensional structure modelling, structure comparison with the enzyme from Staphylococcus aureus, overview
additional information
-
three-dimensional structure modelling, structure comparison with the enzyme from Staphylococcus aureus, overview
additional information
three-dimensional structure of Mtb ICDH-1, overview
additional information
-
three-dimensional structure of Mtb ICDH-1, overview
additional information
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three-dimensional structure of Mtb ICDH-1, overview
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additional information
three-dimensional structure modelling, structure comparison with the human enzyme, PDB IDs 1T09 and 1T0L, overview
additional information
-
three-dimensional structure modelling, structure comparison with the human enzyme, PDB IDs 1T09 and 1T0L, overview
additional information
-
three-dimensional structure modelling, structure comparison with the human enzyme, PDB IDs 1T09 and 1T0L, overview
-
additional information
the overall fold of the enzyme protein is resolved into large domain, small domain and a clasp domain. The monomeric structure reveals also a unique terminal domain involved in dimerization. The overall TtIDH structure exhibits a closed conformation with the conserved catalytic triad residues Tyr144, Asp248, and Lys191. Oligomerization of the protein is determined using interface area and subunitsubunit interactions between protomers
additional information
-
the overall fold of the enzyme protein is resolved into large domain, small domain and a clasp domain. The monomeric structure reveals also a unique terminal domain involved in dimerization. The overall TtIDH structure exhibits a closed conformation with the conserved catalytic triad residues Tyr144, Asp248, and Lys191. Oligomerization of the protein is determined using interface area and subunitsubunit interactions between protomers