Lineage for d2ftyd1 (2fty D:2-56,D:441-541)

  1. Root: SCOPe 2.06
  2. 2017114Class b: All beta proteins [48724] (177 folds)
  3. 2073462Fold 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. 2073463Superfamily 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. 2073524Family b.92.1.3: Hydantoinase (dihydropyrimidinase) [75044] (5 protein domains)
  6. 2073558Protein Dihydropyrimidine amidohydrolase Pyd2 [141683] (2 species)
  7. 2073561Species Yeast (Saccharomyces kluyveri) [TaxId:4934] [141684] (3 PDB entries)
    Uniprot Q9P903 2-56,441-541
  8. 2073573Domain d2ftyd1: 2fty D:2-56,D:441-541 [134093]
    Other proteins in same PDB: d2ftya2, d2ftyb2, d2ftyc2, d2ftyd2
    automated match to d2ftya1
    complexed with zn

Details for d2ftyd1

PDB Entry: 2fty (more details), 2.4 Å

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

SCOPe Domain Sequences for d2ftyd1:

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

>d2ftyd1 b.92.1.3 (D:2-56,D:441-541) Dihydropyrimidine amidohydrolase Pyd2 {Yeast (Saccharomyces kluyveri) [TaxId: 4934]}

SCOPe Domain Coordinates for d2ftyd1:

Click to download the PDB-style file with coordinates for d2ftyd1.
(The format of our PDB-style files is described here.)

Timeline for d2ftyd1: