Lineage for d2ftya1 (2fty A:2-56,A:441-541)

  1. Root: SCOPe 2.08
  2. 2739516Class b: All beta proteins [48724] (180 folds)
  3. 2819141Fold b.92: Composite domain of metallo-dependent hydrolases [51337] (1 superfamily)
    pseudobarrel; mixed sheet of 7 strand folded upon itself and "buckled" by two beta-turns
  4. 2819142Superfamily b.92.1: Composite domain of metallo-dependent hydrolases [51338] (12 families) (S)
    this domain is interrupted by the catalytic beta/alpha barrel domain
  5. 2819203Family b.92.1.3: Hydantoinase (dihydropyrimidinase) [75044] (5 proteins)
  6. 2819237Protein Dihydropyrimidine amidohydrolase Pyd2 [141683] (2 species)
  7. 2819240Species Yeast (Saccharomyces kluyveri) [TaxId:4934] [141684] (3 PDB entries)
    Uniprot Q9P903 2-56,441-541
  8. 2819249Domain d2ftya1: 2fty A:2-56,A:441-541 [134087]
    Other proteins in same PDB: d2ftya2, d2ftyb2, d2ftyc2, d2ftyd2
    complexed with zn

Details for d2ftya1

PDB Entry: 2fty (more details), 2.4 Å

PDB Description: Crystal structure of dihydropyrimidinase from Saccharomyces kluyveri
PDB Compounds: (A:) dihydropyrimidinase

SCOPe Domain Sequences for d2ftya1:

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

>d2ftya1 b.92.1.3 (A:2-56,A:441-541) Dihydropyrimidine amidohydrolase Pyd2 {Yeast (Saccharomyces kluyveri) [TaxId: 4934]}

SCOPe Domain Coordinates for d2ftya1:

Click to download the PDB-style file with coordinates for d2ftya1.
(The format of our PDB-style files is described here.)

Timeline for d2ftya1: