SCOP 1.73: Domain d1vfua3: 1vfu A:121-502

Lineage for d1vfua3 (1vfu A:121-502)

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 Maltogenic amylase, central domain [51465] (4 species)
   contains an additional N-terminal domain

7. Species Thermoactinomyces vulgaris, TVAII [TaxId:2026] [51467] (16 PDB entries)

8. Domain d1vfua3: 1vfu A:121-502 [120057]
   Other proteins in same PDB: d1vfua1, d1vfua2, d1vfub1, d1vfub2
   automatically matched to d1bvza3
   complexed with ca, glc; mutant

Details for d1vfua3

PDB Entry: 1vfu, 3.1 Å

PDB Description: crystal structure of thermoactinomyces vulgaris r-47 amylase 2/gamma- cyclodextrin complex

PDB Compounds: (A:) Neopullulanase 2

SCOP Domain Sequences for d1vfua3:

Sequence; same for both SEQRES and ATOM records:

>d1vfua3 c.1.8.1 (A:121-502) Maltogenic amylase, central domain {Thermoactinomyces vulgaris, TVAII [TaxId: 2026]}
vfttpewakeaviyqifperfangdpsndppgteqwakdarprhdsfyggdlkgvidrlp
yleelgvtalyftpifaspshhkydtadylaidpqfgdlptfrrlvdeahrrgikiilda
vfnhagdqffafrdvlqkgeqsrykdwffiedfpvsktsrtnyetfavqvpampklrten
pevkeylfdvarfwmeqgidgwrlnvanevdhafwrefrrlvkslnpdalivgeiwhdas
gwlmgdqfdsvmnylfresvirffatgeihaerfdaeltrarmlypeqaaqglwnlldsh
nterfltscggneakfrlavlfqmtylgtpliyygdeigmagatdpdcrrpmiweekeqn
rglfefykelirlrhrlasltr

Timeline for d1vfua3:

• d1vfua3 is new in SCOP 1.73
  
• d1vfua3 appears in SCOP 1.75
  
• d1vfua3 appears in the current release, SCOPe 2.08