Lineage for d2fvmc1 (2fvm C:2-56,C:441-541)

  1. Root: SCOPe 2.08
  2. Class b: All beta proteins [48724] (180 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] (12 families) (S)
    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 d2fvmc1: 2fvm C:2-56,C:441-541 [134216]
    Other proteins in same PDB: d2fvma2, d2fvmb2, d2fvmc2, d2fvmd2
    automated match to d2ftya1
    complexed with urp, zn

Details for d2fvmc1

PDB Entry: 2fvm (more details), 2.45 Å

PDB Description: Crystal structure of dihydropyrimidinase from Saccharomyces kluyveri in complex with the reaction product N-carbamyl-beta-alanine
PDB Compounds: (C:) dihydropyrimidinase

SCOPe Domain Sequences for d2fvmc1:

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

>d2fvmc1 b.92.1.3 (C:2-56,C:441-541) Dihydropyrimidine amidohydrolase Pyd2 {Yeast (Saccharomyces kluyveri) [TaxId: 4934]}

SCOPe Domain Coordinates for d2fvmc1 are not available.

Timeline for d2fvmc1:

View in 3D
Domains from same chain:
(mouse over for more information)
View in 3D
Domains from other chains:
(mouse over for more information)
d2fvma1, d2fvma2, d2fvmb1, d2fvmb2, d2fvmd1, d2fvmd2