Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
Fold c.1: TIM beta/alpha-barrel [51350] (34 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] (19 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) automatically mapped to Pfam PF01979 |
Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain [82262] (3 species) |
Species Escherichia coli [TaxId:562] [141808] (4 PDB entries) Uniprot P0AF18 54-350 |
Domain d2p50a2: 2p50 A:54-350 [149224] Other proteins in same PDB: d2p50a1, d2p50b1, d2p50c1, d2p50d1 automated match to d1ymya2 complexed with zn |
PDB Entry: 2p50 (more details), 2.2 Å
SCOPe Domain Sequences for d2p50a2:
Sequence; same for both SEQRES and ATOM records: (download)
>d2p50a2 c.1.9.10 (A:54-350) N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain {Escherichia coli [TaxId: 562]} gfidvqlngcggvqfndtaeavsvetleimqkaneksgctnylptlittsdelmkqgvrv mreylakhpnqalglhlegpwlnlvkkgthnpnfvrkpdaalvdflcenadvitkvtlap emvpaevisklanagivvsaghsnatlkeakagfragitfathlynampyitgrepglag aildeadiycgiiadglhvdyanirnakrlkgdklclvtdatapaganieqfifagktiy yrnglcvdengtlsgssltmiegvrnlvehcgialdevlrmatlyparaigvekrlg
Timeline for d2p50a2: