SCOP 1.73: Domain d2ftyd1: 2fty D:2-56,D:441-541

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

1. Root: SCOP 1.73

2. Class b: All beta proteins [48724] (165 folds)

3. Fold 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. Superfamily b.92.1: Composite domain of metallo-dependent hydrolases [51338] (8 families)
   this domain is interrupted by the catalytic beta/alpha barrel domain

5. Family b.92.1.3: Hydantoinase (dihydropyrimidinase) [75044] (5 proteins)

6. Protein Dihydropyrimidine amidohydrolase Pyd2 [141683] (2 species)

7. Species Yeast (Saccharomyces kluyveri) [TaxId:4934] [141684] (3 PDB entries)

8. Domain 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, 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:

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

Timeline for d2ftyd1:

• d2ftyd1 is new in SCOP 1.73
  
• d2ftyd1 appears in SCOP 1.75
  
• d2ftyd1 appears in the current release, SCOPe 2.08