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.
?
-
x * 46170, amino acid analysis
?
-
x * 49390, calculated, x * 49400, DS-PAGE
?
-
x * 55500, SDS-PAGE, alpha-holoenzyme
?
-
x * 53000, SDS-PAGE, beta-holoenzyme
?
-
x * 46000, SDS-PAGE
-
?
-
x * 47000, gel filtration
?
-
x * 47169, amino acid analysis
hexamer
6 * 46000, SDS-PAGE
hexamer
6 * 46170, calculated from sequence
hexamer
-
6 * 46170, calculated from sequence
-
hexamer
-
x * 50000, SDS-PAGE
hexamer
-
x * 50000, SDS-PAGE
-
hexamer
-
6 x 50000, SDS-PAGE
hexamer
6 * 52800, calculated from sequence of His-tagged recombinant protein
hexamer
-
6 * 52800, calculated from sequence of His-tagged recombinant protein
-
hexamer
EcGDH is a hexamer with 32 symmetry, an assembly. Protomer F (EcGDH-F) is the only molecule in the hexamer that adopts an open conformation that is sufficiently wide for diffusion of both substrate and cofactor, structure comparison to the enzyme from Clostridium symbiosum and other GDHs, overview
hexamer
-
6 * 55000, SDS-PAGE
hexamer
-
6 * 55000, SDS-PAGE
-
hexamer
-
6 * 52000, SDS-PAGE
hexamer
-
6 * 52000, SDS-PAGE
-
hexamer
-
crystallography
hexamer
6 * 52546, GDH1, sequence calculation
hexamer
6 * 54024, GDH2, sequence calculation
hexamer
6 * 47700, tagged recombinant enzyme, SDS-PAGE
hexamer
6 * 47700, calculated
hexamer
-
6 * 47700, calculated
-
hexamer
-
6 * 47700, tagged recombinant enzyme, SDS-PAGE
-
hexamer
-
6 * 44000, SDS-PAGE
hexamer
6 * 45000, SDS-PAGE
homohexamer
-
4 * 43000, isozyme GDHI', SDS-PAGE
homohexamer
-
4 * 43000, isozyme GDHI', SDS-PAGE
-
homohexamer
-
alpha6, 6 * 56000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 46000, SDS-PAGE
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 52000, SDS-PAGE
homohexamer
-
alpha6, 6 * 52000, SDS-PAGE
-
homohexamer
6 * 47000, SDS-PAGE
homohexamer
6 * 49000, SDS-PAGE
homohexamer
-
6 * 47000, SDS-PAGE
-
homohexamer
-
6 * 49000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 46000, SDS-PAGE
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
homohexamer
-
alpha6, 6 * 52000, SDS-PAGE
homohexamer
-
alpha6, 6 * 44500, SDS-PAGE
homohexamer
-
alpha6, 6 * 50000, SDS-PAGE
homohexamer
-
alpha6, 6 * 50120, MALDI-TOF
homohexamer
-
alpha6, 6 * 46500, SDS-PAGE
homohexamer
-
alpha6, 6 * 55000, SDS-PAGE
homohexamer
-
alpha6, 6 * 48000, CTAB-PAGE
homohexamer
-
alpha6, 6 * 55000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 48000, CTAB-PAGE
-
homohexamer
-
alpha6, 6 * 50000, SDS-PAGE
homohexamer
-
alpha6, 6 * 50000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
homohexamer
-
alpha6, 6 * 40000, SDS-PAGE
homohexamer
-
alpha6, 6 * 40000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 56000, SDS-PAGE
homohexamer
-
alpha6, 6 * 56000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 49285, amino acid analysis
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 49285, amino acid analysis
-
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47300, SDS-PAGE
homohexamer
-
alpha6, 6 * 45000, SDS-PAGE, expressed in Escherichia coli
homohexamer
-
alpha6, 6 * 45000, SDS-PAGE
homohexamer
-
alpha6, 6 * 43000, SDS-PAGE
homohexamer
-
alpha6, 6 * ?, crystallization
homotetramer
-
alpha4, 4 * 53500, SDS-PAGE
homotetramer
-
4 * 43000, isozymes GDHI and GDHII, SDS-PAGE
homotetramer
-
4 * 43000, isozymes GDHI and GDHII, SDS-PAGE
-
homotetramer
-
alpha4, 4 * 49000, SDS-PAGE
homotetramer
-
alpha4, 4 * 46000, SDS-PAGE
homotetramer
-
alpha4, 4 * 47000, SDS-PAGE
homotetramer
-
4 * 64000, SDS-PAGE
tetramer
-
4 * 51400, SDS-PAGE
tetramer
-
4 * 51400, SDS-PAGE
-
additional information
modelling of NADP+ in domain II reveals the potential contribution of positively charged residues from a neighbouring alpha-helical hairpin to phosphate recognition, sequence-structure relationship, overview
additional information
the subunit interactions are mediated by networks of salt bridges and hydrogen bonds, monome-monomer interaction, overview
additional information
the subunit interactions are mediated by networks of salt bridges and hydrogen bonds, monome-monomer interaction, overview
additional information
the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The subunit interactions are mainly assisted by hydrogen bonds and hydrophobic interactions, monome-monomer interaction, overview
additional information
the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The subunit interactions are mainly assisted by hydrogen bonds and hydrophobic interactions, monome-monomer interaction, overview