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

  1. Root: SCOPe 2.06
  2. 2078559Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2078560Fold 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
  4. 2084338Superfamily 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. 2084618Family c.1.9.6: Hydantoinase (dihydropyrimidinase), catalytic domain [75073] (5 protein domains)
    automatically mapped to Pfam PF13147
  6. 2084619Protein D-hydantoinase [75074] (4 species)
  7. 2084620Species Bacillus sp. AR9 [TaxId:301298] [141802] (1 PDB entry)
    Uniprot Q5DLU2 2-460
  8. 2084621Domain 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]}

SCOPe Domain Coordinates for d1ynya2:

Click to download the PDB-style file with coordinates for d1ynya2.
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Timeline for d1ynya2:

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