![]() | Class c: Alpha and beta proteins (a/b) [51349] (141 folds) |
![]() | Fold c.1: TIM beta/alpha-barrel [51350] (33 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.1.9: Metallo-dependent hydrolases [51556] (15 families) ![]() the beta-sheet barrel is similarly distorted and capped by a C-terminal helix has transition metal ions bound inside the barrel |
![]() | Family c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain [82261] (1 protein) |
![]() | Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain [82262] (3 species) |
![]() | Bacillus subtilis [TaxId:1423] [102086] (1 PDB entry) |
![]() | Domain d1un7a2: 1un7 A:58-358 [99658] Other proteins in same PDB: d1un7a1, d1un7b1 |
![]() | Domain d1un7b2: 1un7 B:58-358 [99660] Other proteins in same PDB: d1un7a1, d1un7b1 complexed with 2pe, fe, glp |
![]() | Escherichia coli [TaxId:562] [141808] (2 PDB entries) |
![]() | Domain d1ymya2: 1ymy A:54-350 [123709] Other proteins in same PDB: d1ymya1, d1ymyb1 |
![]() | Domain d1ymyb2: 1ymy B:54-350 [123711] Other proteins in same PDB: d1ymya1, d1ymyb1 automatically matched to 1YMY A:54-350 |
![]() | Domain d1yrra2: 1yrr A:54-350 [123936] Other proteins in same PDB: d1yrra1, d1yrrb1 automatically matched to 1YMY A:54-350 complexed with gol, po4 |
![]() | Domain d1yrrb2: 1yrr B:54-350 [123938] Other proteins in same PDB: d1yrra1, d1yrrb1 automatically matched to 1YMY A:54-350 complexed with gol, po4 |
![]() | Thermotoga maritima [TaxId:2336] [82263] (1 PDB entry) TM0814 |
![]() | Domain d1o12a2: 1o12 A:44-331 [80759] Other proteins in same PDB: d1o12a1, d1o12b1 |
![]() | Domain d1o12b2: 1o12 B:44-331 [80761] Other proteins in same PDB: d1o12a1, d1o12b1 structural genomics CASP5 complexed with fe, mse |
Timeline for Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain from c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain: