SCOPe 2.04: Domain d2fvma1: 2fvm A:2-56,A:441-541

Lineage for d2fvma1 (2fvm A:2-56,A:441-541)

1. Root: SCOPe 2.04

2. Class b: All beta proteins [48724] (176 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)
   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 d2fvma1: 2fvm A:2-56,A:441-541 [134212]
   Other proteins in same PDB: d2fvma2, d2fvmb2, d2fvmc2, d2fvmd2
   automated match to d2ftya1
   complexed with urp, zn

Details for d2fvma1

PDB Entry: 2fvm, 2.45 Å

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

PDB Compounds: (A:) dihydropyrimidinase

SCOPe Domain Sequences for d2fvma1:

Sequence; same for both SEQRES and ATOM records:

>d2fvma1 b.92.1.3 (A:2-56,A:441-541) Dihydropyrimidine amidohydrolase Pyd2 {Yeast (Saccharomyces kluyveri) [TaxId: 4934]}
piydliikngiictasdiyaaeiavnngkvqliaasidpslgsevidaegafitpXilpg
vsdadlviwypddskkeynskpklitnklmehncdytpfegieiknwprytivkgkivyk
egeilkenadgkylkrgksfmctpknewvtewrpkye

Timeline for d2fvma1:

• d2fvma1 first appeared in SCOP 1.73
  
• d2fvma1 appears in SCOPe 2.03
  
• d2fvma1 appears in SCOPe 2.05
  
• d2fvma1 appears in the current release, SCOPe 2.08