SCOP 1.71: Family d.2.1.6: Bacterial muramidase, catalytic domain

Lineage for Family d.2.1.6: Bacterial muramidase, catalytic domain

1. Root: SCOP 1.71

2. Class d: Alpha and beta proteins (a+b) [53931] (286 folds)

3. Fold d.2: Lysozyme-like [53954] (1 superfamily)
   common alpha+beta motif for the active site region

4. Superfamily d.2.1: Lysozyme-like [53955] (7 families)

5. Family d.2.1.6: Bacterial muramidase, catalytic domain [53991] (2 proteins)
   the large N-terminal domain is all-alpha superhelix

Proteins:

1. 36 kDa soluble lytic transglycosylase, SLT35 [53994] (1 species)

   • Species Escherichia coli [TaxId:562] [53995] (8 PDB entries)

2. 70 kDa soluble lytic transglycosylase, SLT70 [53992] (1 species)

   • Species Escherichia coli [TaxId:562] [53993] (3 PDB entries)

More info for Family d.2.1.6: Bacterial muramidase, catalytic domain

Timeline for Family d.2.1.6: Bacterial muramidase, catalytic domain:

• Family d.2.1.6: Bacterial muramidase, catalytic domain first appeared (with stable ids) in SCOP 1.55
  
• Family d.2.1.6: Bacterial muramidase, catalytic domain appears in SCOP 1.69
  
• Family d.2.1.6: Bacterial muramidase, catalytic domain appears in SCOP 1.73
  
• Family d.2.1.6: Bacterial muramidase, catalytic domain appears in the current release, SCOPe 2.08