SCOP 1.71: Domain d1mfua2: 1mfu A:1-403

Lineage for d1mfua2 (1mfu A:1-403)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (32 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.1.8: (Trans)glycosidases [51445] (13 families)

5. Family c.1.8.1: Amylase, catalytic domain [51446] (24 proteins)
   members of the family may contain various insert subdomains
   in alpha-amylases and closer relatives this domain is usually followed by a common all-beta domain

6. Protein Animal alpha-amylase [51458] (3 species)
   contains Ca2+-binding subdomain, residues 100-170

7. Species Human (Homo sapiens) [TaxId:9606] [51460] (27 PDB entries)

8. Domain d1mfua2: 1mfu A:1-403 [79048]
   Other proteins in same PDB: d1mfua1
   complexed with agl, ca, cl, glc, hmc, pca; mutant

Details for d1mfua2

PDB Entry: 1mfu, 2 Å

PDB Description: probing the role of a mobile loop in human salivary amylase: structural studies on the loop-deleted mutant

SCOP Domain Sequences for d1mfua2:

Sequence; same for both SEQRES and ATOM records:

>d1mfua2 c.1.8.1 (A:1-403) Animal alpha-amylase {Human (Homo sapiens)}
eyssntqqgrtsivhlfewrwvdialecerylapkgfggvqvsppnenvaihnpfrpwwe
ryqpvsyklctrsgnedefrnmvtrcnnvgvriyvdavinhmcgnavsagtsstcgsyfn
pgsrdfpavpysgwdfndgkcktgsgdienyndatqvrdcrlsglldlalgkdyvrskia
eymnhlidigvagfridaskhmwpgdikaildklhnlnsnwfpegskpfiyqevidlgge
pikssdyfgngrvtefkygaklgtvirkwngekmsylknwgegwgfmpsdralvfvdnhd
nqrghsiltfwdarlykmavgfmlahpygftrvmssyrwpryfengkdvndwvgppndng
vtkevtinpdttcgndwvcehrwrqirnmvnfrnvvdgqpftn

Timeline for d1mfua2:

• d1mfua2 first appeared in SCOP 1.63
  
• d1mfua2 appears in SCOP 1.69
  
• d1mfua2 appears in SCOP 1.73
  
• d1mfua2 appears in the current release, SCOPe 2.08