SCOPe 2.01: Domain d2fvka1: 2fvk A:2-56,A:441-541

Lineage for d2fvka1 (2fvk A:2-56,A:441-541)

1. Root: SCOPe 2.01

2. Class b: All beta proteins [48724] (174 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] (11 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)
   Uniprot Q9P903 2-56,441-541

8. Domain d2fvka1: 2fvk A:2-56,A:441-541 [134204]
   Other proteins in same PDB: d2fvka2, d2fvkb2, d2fvkc2, d2fvkd2
   automatically matched to 2FTY A:2-56,A:441-541
   complexed with duc, zn

Details for d2fvka1

PDB Entry: 2fvk, 2.4 Å

PDB Description: Crystal structure of dihydropyrimidinase from Saccharomyces kluyveri in complex with the substrate dihydrouracil

PDB Compounds: (A:) dihydropyrimidinase

SCOPe Domain Sequences for d2fvka1:

Sequence; same for both SEQRES and ATOM records:

>d2fvka1 b.92.1.3 (A:2-56,A:441-541) Dihydropyrimidine amidohydrolase Pyd2 {Yeast (Saccharomyces kluyveri) [TaxId: 4934]}
piydliikngiictasdiyaaeiavnngkvqliaasidpslgsevidaegafitpXilpg
vsdadlviwypddskkeynskpklitnklmehncdytpfegieiknwprytivkgkivyk
egeilkenadgkylkrgksfmctpknewvtewrpkye

Timeline for d2fvka1:

• d2fvka1 first appeared in SCOP 1.73
  
• d2fvka1 appears in SCOP 1.75
  
• d2fvka1 appears in SCOPe 2.02
  
• d2fvka1 appears in the current release, SCOPe 2.08