SCOPe 2.01: Domain d1ob0a1: 1ob0 A:394-483

Lineage for d1ob0a1 (1ob0 A:394-483)

1. Root: SCOPe 2.01

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] (5 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 Bacterial alpha-Amylase [51013] (9 species)

7. Species Bacillus licheniformis [TaxId:1402] [51014] (8 PDB entries)

8. Domain d1ob0a1: 1ob0 A:394-483 [81256]
   Other proteins in same PDB: d1ob0a2
   complexed with ca, na

Details for d1ob0a1

PDB Entry: 1ob0, 1.83 Å

PDB Description: kinetic stabilization of bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface

PDB Compounds: (A:) alpha-amylase

SCOPe Domain Sequences for d1ob0a1:

Sequence; same for both SEQRES and ATOM records:

>d1ob0a1 b.71.1.1 (A:394-483) Bacterial alpha-Amylase {Bacillus licheniformis [TaxId: 1402]}
yaygaqhdyfdhhdivgwtregdssvansglaalitdgpggakrmyvgrqnagetwhdit
gnrsepvvinsegwgefhvnggsvsiyvqr

Timeline for d1ob0a1:

• d1ob0a1 first appeared in SCOP 1.63
  
• d1ob0a1 appears in SCOP 1.75
  
• d1ob0a1 appears in SCOPe 2.02
  
• d1ob0a1 appears in the current release, SCOPe 2.08