SCOPe 2.05: Domain d1ud3a2: 1ud3 A:1-390

Lineage for d1ud3a2 (1ud3 A:1-390)

1. Root: SCOPe 2.05

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (15 families)

5. Family c.1.8.1: Amylase, catalytic domain [51446] (26 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 Bacterial alpha-amylase [51447] (10 species)

7. Species Bacillus sp., ksm-k38 [TaxId:1409] [89463] (6 PDB entries)

8. Domain d1ud3a2: 1ud3 A:1-390 [88472]
   Other proteins in same PDB: d1ud3a1
   complexed with na; mutant

Details for d1ud3a2

PDB Entry: 1ud3, 2.15 Å

PDB Description: crystal structure of amyk38 n289h mutant

PDB Compounds: (A:) amylase

SCOPe Domain Sequences for d1ud3a2:

Sequence; same for both SEQRES and ATOM records:

>d1ud3a2 c.1.8.1 (A:1-390) Bacterial alpha-amylase {Bacillus sp., ksm-k38 [TaxId: 1409]}
dglngtmmqyyewhlendgqhwnrlhddaaalsdagitaiwippaykgnsqadvgygayd
lydlgefnqkgtvrtkygtkaqleraigslksndinvygdvvmnhkmgadfteavqavqv
nptnrwqdisgaytidawtgfdfsgrnnaysdfkwrwfhfngvdwdqryqenhifrfant
nwnwrvdeengnydyllgsnidfshpevqdelkdwgswftdeldldgyrldaikhipfwy
tsdwvrhqrneadqdlfvvgeywkddvgalefyldemnwemslfdvplhynfyrasqqgg
sydmrnilrgslveahpmhavtfvdnhdtqpgesleswvadwfkplayatiltreggypn
vfygdyygipndnisakkdmidelldarqn

Timeline for d1ud3a2:

• d1ud3a2 first appeared in SCOP 1.65
  
• d1ud3a2 appears in SCOPe 2.04
  
• d1ud3a2 appears in SCOPe 2.06
  
• d1ud3a2 appears in the current release, SCOPe 2.08