Class c: Alpha and beta proteins (a/b) [51349] (130 folds) |
Fold c.1: TIM beta/alpha-barrel [51350] (28 superfamilies) contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites |
Superfamily c.1.10: Aldolase [51569] (5 families) Common fold covers whole protein structure |
Family c.1.10.1: Class I aldolase [51570] (10 proteins) the catalytic lysine forms schiff-base intermediate with substrate possible link between the aldolase superfamily and the phosphate-binding beta/alpha barrels |
Protein KDPG aldolase [51584] (2 species) |
Species Escherichia coli [TaxId:562] [51585] (4 PDB entries) |
Domain d1euaa_: 1eua A: [29155] |
Domain d1euab_: 1eua B: [29156] |
Domain d1euac_: 1eua C: [29157] Schiff base intermediate complexed with act, pyr, so4 |
Domain d1euna_: 1eun A: [29158] |
Domain d1eunb_: 1eun B: [29159] |
Domain d1eunc_: 1eun C: [29160] complexed with so4 |
Domain d1fq0a_: 1fq0 A: [29161] |
Domain d1fq0b_: 1fq0 B: [29162] |
Domain d1fq0c_: 1fq0 C: [29163] complexed with cit |
Domain d1fwra_: 1fwr A: [29164] |
Domain d1fwrb_: 1fwr B: [29165] |
Domain d1fwrc_: 1fwr C: [29166] complexed with cit; mutant |
Timeline for Species Escherichia coli [TaxId:562] from c.1.10.1 KDPG aldolase: