Lineage for d1ynya2 (1yny A:53-384)

  1. Root: SCOPe 2.08
  2. 2826024Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2826025Fold c.1: TIM beta/alpha-barrel [51350] (34 superfamilies)
    contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
    the first seven superfamilies have similar phosphate-binding sites
  4. 2833366Superfamily c.1.9: Metallo-dependent hydrolases [51556] (19 families) (S)
    the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
    has transition metal ions bound inside the barrel
  5. 2833715Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (5 proteins)
    automatically mapped to Pfam PF13147
  6. 2833716Protein D-hydantoinase [75074] (4 species)
  7. 2833717Species Bacillus sp. AR9 [TaxId:301298] [141802] (1 PDB entry)
    Uniprot Q5DLU2 2-460
  8. 2833718Domain d1ynya2: 1yny A:53-384 [123765]
    Other proteins in same PDB: d1ynya1, d1ynyb1
    complexed with mn

Details for d1ynya2

PDB Entry: 1yny (more details), 2.3 Å

PDB Description: molecular structure of d-hydantoinase from a bacillus sp. ar9: evidence for mercury inhibition
PDB Compounds: (A:) D-hydantoinase

SCOPe Domain Sequences for d1ynya2:

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

>d1ynya2 c.1.9.6 (A:53-384) D-hydantoinase {Bacillus sp. AR9 [TaxId: 301298]}
ggidphthldmpfggtvtaddfftgtraaafggttsivdfcltkkgeslksaiatwheka
rgkavidygfhlmiaeandqvleelesvissegitslkvfmayknvfqaddetlfktlvk
akelgalvqvhaengdvldyltkkalaegntdpiyhaytrppeaegeatgraialtalag
sqlyvvhvscasavqriaearekgwnvygetcpqylaldvsimdqpdfegakyvwspplr
ekwnqevlwsalkngilqtvgsdhcpfnfrgqkelgrgdftkipnggpliedrltilyse
gvrqgrislnqfvdisstkaaklfgmfprkgt

SCOPe Domain Coordinates for d1ynya2:

Click to download the PDB-style file with coordinates for d1ynya2.
(The format of our PDB-style files is described here.)

Timeline for d1ynya2:

2833718
d1ynya2 in context of chain
View in 3D
Domains from same chain:
(mouse over for more information)
d1ynya1