SCOPe 2.03: Domain d1vfma2: 1vfm A:503-585

Lineage for d1vfma2 (1vfm A:503-585)

1. Root: SCOPe 2.03

2. Class b: All beta proteins [48724] (174 folds)

3. Fold b.71: Glycosyl hydrolase domain [51010] (1 superfamily)
   folded sheet; greek-key

4. Superfamily b.71.1: Glycosyl hydrolase domain [51011] (6 families)
   this domain is C-terminal to the catalytic beta/alpha barrel domain

5. Family b.71.1.1: alpha-Amylases, C-terminal beta-sheet domain [51012] (22 proteins)
   this domain follows the catalytic beta/alpha barrel domain

6. Protein Maltogenic amylase [51031] (4 species)

7. Species Thermoactinomyces vulgaris, TVAII [TaxId:2026] [51033] (16 PDB entries)

8. Domain d1vfma2: 1vfm A:503-585 [120043]
   Other proteins in same PDB: d1vfma1, d1vfma3, d1vfmb1, d1vfmb3
   automatically matched to d1bvza2
   complexed with ca

Details for d1vfma2

PDB Entry: 1vfm, 2.9 Å

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

PDB Compounds: (A:) Neopullulanase 2

SCOPe Domain Sequences for d1vfma2:

Sequence; same for both SEQRES and ATOM records:

>d1vfma2 b.71.1.1 (A:503-585) Maltogenic amylase {Thermoactinomyces vulgaris, TVAII [TaxId: 2026]}
gnvrswhadkqanlyafvrtvqdqhvgvvlnnrgekqtvllqvpesggktwldcltgeev
hgkqgqlkltlrpyqgmilwngr

Timeline for d1vfma2:

• d1vfma2 first appeared in SCOP 1.73
  
• d1vfma2 appears in SCOPe 2.02
  
• d1vfma2 appears in SCOPe 2.04
  
• d1vfma2 appears in the current release, SCOPe 2.08