Lineage for d2ylsa1 (2yls A:11-154,A:390-542)

  1. Root: SCOPe 2.06
  2. 2089713Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2109341Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
    core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander
  4. 2109342Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families) (S)
  5. 2109874Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (15 proteins)
    duplication: both domains have similar folds and functions
    most members of the family contain common C-terminal alpha+beta domain
  6. 2110118Protein Phenylacetone monooxygenase [110440] (1 species)
  7. 2110119Species Thermobifida fusca [TaxId:2021] [110441] (6 PDB entries)
    Uniprot Q5YS95 # 55% sequence identity; Nocardia farcinica TaxID:37329
  8. 2110122Domain d2ylsa1: 2yls A:11-154,A:390-542 [207665]
    automated match to d1w4xa1
    complexed with fad, nap

Details for d2ylsa1

PDB Entry: 2yls (more details), 2.26 Å

PDB Description: snapshots of enzymatic baeyer-villiger catalysis: oxygen activation and intermediate stabilization: reduced enzyme bound to nadp
PDB Compounds: (A:) phenylacetone monooxygenase

SCOPe Domain Sequences for d2ylsa1:

Sequence; same for both SEQRES and ATOM records: (download)

>d2ylsa1 c.3.1.5 (A:11-154,A:390-542) Phenylacetone monooxygenase {Thermobifida fusca [TaxId: 2021]}

SCOPe Domain Coordinates for d2ylsa1:

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Timeline for d2ylsa1:

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