Class c: Alpha and beta proteins (a/b) [51349] (147 folds) |
Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies) contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites |
Superfamily c.1.9: Metallo-dependent hydrolases [51556] (18 families) the beta-sheet barrel is similarly distorted and capped by a C-terminal helix has transition metal ions bound inside the barrel |
Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (5 proteins) |
Protein Dihydropyrimidine amidohydrolase Pyd2 [141805] (2 species) |
Species Yeast (Saccharomyces kluyveri) [TaxId:4934] [141806] (3 PDB entries) Uniprot Q9P903 57-440 |
Domain d2fvma2: 2fvm A:57-440 [134213] Other proteins in same PDB: d2fvma1, d2fvmb1, d2fvmc1, d2fvmd1 automatically matched to 2FTY A:57-440 complexed with urp, zn |
PDB Entry: 2fvm (more details), 2.45 Å
SCOP Domain Sequences for d2fvma2:
Sequence, based on SEQRES records: (download)
>d2fvma2 c.1.9.6 (A:57-440) Dihydropyrimidine amidohydrolase Pyd2 {Yeast (Saccharomyces kluyveri) [TaxId: 4934]} ggidahvhvdeplkllgdvvdtmehatrsavaggtttvvafstqdvskkgpsalaesvkl dvdeyseqtlycdyglhlilfqiekpsvearelldvqlqaayndygvssvkmfmtypglq isdydimsamyatrkngfttmlhaengdmvkwmiealeeqgltdayyhgvsrpsivegea tnraitlattmdtpilfvhvsspqaaevikqaqtkglkvyaetcpqyallsdaitrchhh gevesygvgidlssisespftnpddrfigskyicsppirpegtqksiwkgmnngtftivg sdhcsynyyektstaskhrafdpennkngefryipnglpgvctrmpllydygylrgnlts mmklveiqctnpakvygmypqkgs
>d2fvma2 c.1.9.6 (A:57-440) Dihydropyrimidine amidohydrolase Pyd2 {Yeast (Saccharomyces kluyveri) [TaxId: 4934]} ggidahvhvdeplkllgdvvdtmehatrsavaggtttvvafstqdvskkgpsalaesvkl dvdeyseqtlycdyglhlilfqiekpsvearelldvqlqaayndygvssvkmfmtypglq isdydimsamyatrkngfttmlhaengdmvkwmiealeeqgltdayyhgvsrpsivegea tnraitlattmdtpilfvhvsspqaaevikqaqtkglkvyaetcpqyallsdaitrchgv gidlssisespftnpddrfigskyicsppirpegtqksiwkgmnngtftivgsdhcsyny yektstaskhrafdpennkngefryipnglpgvctrmpllydygylrgnltsmmklveiq ctnpakvygmypqkgs
Timeline for d2fvma2: