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

  1. Root: SCOP 1.73
  2. 651986Class b: All beta proteins [48724] (165 folds)
  3. 678879Fold 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. 678880Superfamily b.92.1: Composite domain of metallo-dependent hydrolases [51338] (8 families) (S)
    this domain is interrupted by the catalytic beta/alpha barrel domain
  5. 678932Family b.92.1.3: Hydantoinase (dihydropyrimidinase) [75044] (5 proteins)
  6. 678966Protein Dihydropyrimidine amidohydrolase Pyd2 [141683] (2 species)
  7. 678969Species Yeast (Saccharomyces kluyveri) [TaxId:4934] [141684] (3 PDB entries)
  8. 678981Domain d2ftyd1: 2fty D:2-56,D:441-541 [134093]
    Other proteins in same PDB: d2ftya2, d2ftyb2, d2ftyc2, d2ftyd2
    automatically matched to 2FTY A:2-56,A:441-541
    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

SCOP 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]}
piydliikngiictasdiyaaeiavnngkvqliaasidpslgsevidaegafitpXilpg
vsdadlviwypddskkeynskpklitnklmehncdytpfegieiknwprytivkgkivyk
egeilkenadgkylkrgksfmctpknewvtewrpkye

SCOP 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: