SCOPe 2.07: Domain d1rjra3: 1rjr A:62-419

Lineage for d1rjra3 (1rjr A:62-419)

1. Root: SCOPe 2.07

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold 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. Superfamily c.1.9: Metallo-dependent hydrolases [51556] (19 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 d1rjra3: 1rjr A:62-419 [97580]
   Other proteins in same PDB: d1rjra1, d1rjra2
   complexed with act, zn; mutant

Details for d1rjra3

PDB Entry: 1rjr, 2.1 Å

PDB Description: the crystal structure of the d-aminoacylase d366a mutant in complex with 100mm zncl2

PDB Compounds: (A:) D-aminoacylase

SCOPe Domain Sequences for d1rjra3:

Sequence; same for both SEQRES and ATOM records:

>d1rjra3 c.1.9.11 (A:62-419) N-acyl-D-aminoacid amidohydrolase, catalytic domain {Alcaligenes faecalis [TaxId: 511]}
gfidshthddnyllkhrdmtpkisqgvttvvtgncgislaplahanppapldlldeggsf
rfarfsdylealraappavnaacmvghstlraavmpdlrreatadeiqamqaladdalas
gaigistgafyppaahasteeiievcrplithggvyathmrdegehivqaleetfrigre
ldvpvvishhkvmgklnfgrsketlalieaamasqdvsldaypyvagstmlkqdrvllag
rtlitwckpypelsgrdleeiaaergkskydvvpelqpagaiyfmmdepdvqrilafgpt
migsaglphderphprlwgtfprvlghysrdlglfpletavwkmtgltaakfglaerg

Timeline for d1rjra3:

• d1rjra3 first appeared in SCOP 1.67
  
• d1rjra3 appears in SCOPe 2.06
  
• d1rjra3 appears in the current release, SCOPe 2.08