SCOPe 2.05: Domain d2aaaa1: 2aaa A:382-476

Lineage for d2aaaa1 (2aaa A:382-476)

1. Root: SCOPe 2.05

2. Class b: All beta proteins [48724] (176 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 Fungal alpha-amylase [51028] (2 species)

7. Species Aspergillus niger, acid amylase [TaxId:5061] [51029] (1 PDB entry)

8. Domain d2aaaa1: 2aaa A:382-476 [27777]
   Other proteins in same PDB: d2aaaa2
   complexed with ca

Details for d2aaaa1

PDB Entry: 2aaa, 2.12 Å

PDB Description: calcium binding in alpha-amylases: an x-ray diffraction study at 2.1 angstroms resolution of two enzymes from aspergillus

PDB Compounds: (A:) alpha-amylase

SCOPe Domain Sequences for d2aaaa1:

Sequence; same for both SEQRES and ATOM records:

>d2aaaa1 b.71.1.1 (A:382-476) Fungal alpha-amylase {Aspergillus niger, acid amylase [TaxId: 5061]}
yandafytdsntiamakgtsgsqvitvlsnkgssgssytltlsgsgytsgtklieaytct
svtvdssgdipvpmasglprvllpasvvdssslcg

Timeline for d2aaaa1:

• d2aaaa1 first appeared (with stable ids) in SCOP 1.55, called d2aaa_1
  
• d2aaaa1 appears in SCOPe 2.04
  
• d2aaaa1 appears in SCOPe 2.06
  
• d2aaaa1 appears in the current release, SCOPe 2.08