Lineage for d1v4ya3 (1v4y A:62-419)

  1. Root: SCOP 1.67
  2. 383641Class c: Alpha and beta proteins (a/b) [51349] (130 folds)
  3. 383642Fold c.1: TIM beta/alpha-barrel [51350] (28 superfamilies)
    contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
    the first seven superfamilies have similar phosphate-binding sites
  4. 385405Superfamily c.1.9: Metallo-dependent hydrolases [51556] (13 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. 385570Family c.1.9.11: D-aminoacylase, catalytic domain [82264] (1 protein)
  6. 385571Protein N-acyl-D-aminoacid amidohydrolase, catalytic domain [82265] (1 species)
    contains small a/b subdomain inserted after strand 7; unusual for the superfamily metal coordination by Cys
  7. 385572Species Alcaligenes faecalis [TaxId:511] [82266] (8 PDB entries)
  8. 385576Domain d1v4ya3: 1v4y A:62-419 [100317]
    Other proteins in same PDB: d1v4ya1, d1v4ya2
    complexed with act, zn2; mutant

Details for d1v4ya3

PDB Entry: 1v4y (more details), 1.65 Å

PDB Description: the functional role of the binuclear metal center in d-aminoacylase. one-metal activation and second-metal attenuation

SCOP Domain Sequences for d1v4ya3:

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

>d1v4ya3 c.1.9.11 (A:62-419) N-acyl-D-aminoacid amidohydrolase, catalytic domain {Alcaligenes faecalis}

SCOP Domain Coordinates for d1v4ya3:

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Timeline for d1v4ya3: