Lineage for d1v51a3 (1v51 A:62-419)

  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. 2084801Family c.1.9.11: D-aminoacylase, catalytic domain [82264] (1 protein)
  6. 2084802Protein 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. 2084803Species Alcaligenes faecalis [TaxId:511] [82266] (8 PDB entries)
  8. 2084806Domain d1v51a3: 1v51 A:62-419 [100320]
    Other proteins in same PDB: d1v51a1, d1v51a2
    complexed with act, zn

Details for d1v51a3

PDB Entry: 1v51 (more details), 1.6 Å

PDB Description: The functional role of the binuclear metal center in D-aminoacylase. One-metal activation and second-metal attenuation
PDB Compounds: (A:) D-aminoacylase

SCOPe Domain Sequences for d1v51a3:

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

>d1v51a3 c.1.9.11 (A:62-419) N-acyl-D-aminoacid amidohydrolase, catalytic domain {Alcaligenes faecalis [TaxId: 511]}

SCOPe Domain Coordinates for d1v51a3:

Click to download the PDB-style file with coordinates for d1v51a3.
(The format of our PDB-style files is described here.)

Timeline for d1v51a3: