Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
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 |
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 |
Family c.1.9.11: D-aminoacylase, catalytic domain [82264] (1 protein) |
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 |
Species Alcaligenes faecalis [TaxId:511] [82266] (8 PDB entries) |
Domain d1v51a3: 1v51 A:62-419 [100320] Other proteins in same PDB: d1v51a1, d1v51a2 complexed with act, zn |
PDB Entry: 1v51 (more details), 1.6 Å
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]} gfidshthddnyllkhrdmtpkisqgvttvvtgncgislaplahanppapldlldeggsf rfarfsdylealraappavnaacmvghstlraavmpdlrreatadeiqamqaladdalas gaigistgafyppaahasteeiievcrplithggvyathmrdegehivqaleetfrigre ldvpvvishhkvmgklnfgrsketlalieaamasqdvsldaypyvagstmlkqdrvllag rtlitwckpypelsgrdleeiaaergkskydvvpelqpagaiyfmmdepdvqrilafgpt migsdglphderphprlwgtfprvlghysrdlglfpletavwkmtgltaakfglaerg
Timeline for d1v51a3: