SCOP 1.75: Domain d2p53b2: 2p53 B:54-350

Lineage for d2p53b2 (2p53 B:54-350)

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 folds)

3. 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

4. Superfamily c.1.9: Metallo-dependent hydrolases [51556] (18 families)
   the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
   has transition metal ions bound inside the barrel

5. Family c.1.9.10: N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain [82261] (1 protein)

6. Protein N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain [82262] (3 species)

7. Species Escherichia coli [TaxId:562] [141808] (4 PDB entries)
   Uniprot P0AF18 54-350

8. Domain d2p53b2: 2p53 B:54-350 [149234]
   Other proteins in same PDB: d2p53a1, d2p53b1
   automatically matched to d1ymya2
   complexed with nng, zn; mutant

Details for d2p53b2

PDB Entry: 2p53, 2.1 Å

PDB Description: crystal structure of n-acetyl-d-glucosamine-6-phosphate deacetylase d273n mutant complexed with n-acetyl phosphonamidate-d-glucosamine-6- phosphate

PDB Compounds: (B:) N-acetylglucosamine-6-phosphate deacetylase

SCOP Domain Sequences for d2p53b2:

Sequence; same for both SEQRES and ATOM records:

>d2p53b2 c.1.9.10 (B:54-350) N-acetylglucosamine-6-phosphate deacetylase, NagA, catalytic domain {Escherichia coli [TaxId: 562]}
gfidvqlngcggvqfndtaeavsvetleimqkaneksgctnylptlittsdelmkqgvrv
mreylakhpnqalglhlegpwlnlvkkgthnpnfvrkpdaalvdflcenadvitkvtlap
emvpaevisklanagivvsaghsnatlkeakagfragitfathlynampyitgrepglag
aildeadiycgiiadglhvdyanirnakrlkgdklclvtnatapaganieqfifagktiy
yrnglcvdengtlsgssltmiegvrnlvehcgialdevlrmatlyparaigvekrlg

Timeline for d2p53b2:

• d2p53b2 is new in SCOP 1.75
  
• d2p53b2 appears in SCOPe 2.01
  
• d2p53b2 appears in the current release, SCOPe 2.08