SCOP 1.73: Domain d1eswa_: 1esw A:

Lineage for d1eswa_ (1esw A:)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 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.1.8: (Trans)glycosidases [51445] (14 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 Amylomaltase MalQ [51478] (3 species)
   4-alpha-glucanotransferase; single-domain amylase with several insertions in the common fold

7. Species Thermus aquaticus [TaxId:271] [51479] (4 PDB entries)
   synonym: Thermus thermophilus

8. Domain d1eswa_: 1esw A: [59500]
   complexed with acr, edo

Details for d1eswa_

PDB Entry: 1esw, 1.9 Å

PDB Description: x-ray structure of acarbose bound to amylomaltase from thermus aquaticus. implications for the synthesis of large cyclic glucans

PDB Compounds: (A:) amylomaltase

SCOP Domain Sequences for d1eswa_:

Sequence; same for both SEQRES and ATOM records:

>d1eswa_ c.1.8.1 (A:) Amylomaltase MalQ {Thermus aquaticus [TaxId: 271]}
melprafglllhptslpgpygvgvlgreardflrflkeaggrywqvlplgptgygdspyq
sfsafagnpylidlrplaergyvrledpgfpqgrvdygllyawkwpalkeafrgfkekas
peereafaafrereawwledyalfmalkgahgglpwnrwplplrkreekalreaksalae
evafhaftqwlffrqwgalkaeaealgiriigdmpifvaedsaevwahpewfhldeegrp
tvvagvppdyfsetgqrwgnplyrwdvleregfsfwirrlekalelfhlvridhfrgfea
yweipascptavegrwvkapgeklfqkiqevfgevpvlaedlgvitpevealrdrfglpg
mkvlqfafddgmenpflphnypahgrvvvytgthdndttlgwyrtatphekafmarylad
wgitfreeeevpwalmhlgmksvarlavypvqdvlalgsearmnypgrpsgnwawrllpg
elspehgarlramaeaterl

Timeline for d1eswa_:

• d1eswa_ first appeared in SCOP 1.57
  
• d1eswa_ appears in SCOP 1.71
  
• d1eswa_ appears in SCOP 1.75
  
• d1eswa_ appears in the current release, SCOPe 2.08