SCOP 1.71: Domain d1rk5a3: 1rk5 A:62-419

Lineage for d1rk5a3 (1rk5 A:62-419)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (32 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.9: Metallo-dependent hydrolases [51556] (13 families)
   the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
   has transition metal ions bound inside the barrel

5. Family c.1.9.11: D-aminoacylase, catalytic domain [82264] (1 protein)

6. Protein 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. Species Alcaligenes faecalis [TaxId:511] [82266] (8 PDB entries)

8. Domain d1rk5a3: 1rk5 A:62-419 [97598]
   Other proteins in same PDB: d1rk5a1, d1rk5a2
   complexed with act, cu, zn2; mutant

Details for d1rk5a3

PDB Entry: 1rk5, 1.8 Å

PDB Description: the d-aminoacylase mutant d366a in complex with 100mm cucl2

SCOP Domain Sequences for d1rk5a3:

Sequence; same for both SEQRES and ATOM records:

>d1rk5a3 c.1.9.11 (A:62-419) N-acyl-D-aminoacid amidohydrolase, catalytic domain {Alcaligenes faecalis}
gfidshthddnyllkhrdmtpkisqgvttvvtgncgislaplahanppapldlldeggsf
rfarfsdylealraappavnaacmvghstlraavmpdlrreatadeiqamqaladdalas
gaigistgafyppaahasteeiievcrplithggvyathmrdegehivqaleetfrigre
ldvpvvishhkvmgklnfgrsketlalieaamasqdvsldaypyvagstmlkqdrvllag
rtlitwckpypelsgrdleeiaaergkskydvvpelqpagaiyfmmdepdvqrilafgpt
migsaglphderphprlwgtfprvlghysrdlglfpletavwkmtgltaakfglaerg

Timeline for d1rk5a3:

• d1rk5a3 first appeared in SCOP 1.67
  
• d1rk5a3 appears in SCOP 1.69
  
• d1rk5a3 appears in SCOP 1.73
  
• d1rk5a3 appears in the current release, SCOPe 2.08