![]() | Class c: Alpha and beta proteins (a/b) [51349] (121 folds) |
![]() | Fold c.1: TIM beta/alpha-barrel [51350] (26 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] (13 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.1.9.13: Isoaspartyl dipeptidase, catalytic domain [89489] (1 protein) |
![]() | Protein Isoaspartyl dipeptidase, catalytic domain [89490] (1 species) |
![]() | Species Escherichia coli [TaxId:562] [89491] (2 PDB entries) |
![]() | Domain d1onwb2: 1onw B:63-346 [87175] Other proteins in same PDB: d1onwa1, d1onwb1 complexed with cl, egl, kcx, mg, na, zn |
PDB Entry: 1onw (more details), 1.65 Å
SCOP Domain Sequences for d1onwb2:
Sequence, based on SEQRES records: (download)
>d1onwb2 c.1.9.13 (B:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli} gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal efarkggtiditssidepvapaegiaravqagiplarvtlssdgngsqpffddegnlthi gvagfetlletvqvlvkdydfsisdalrpltssvagflnltgkg
>d1onwb2 c.1.9.13 (B:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli} gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal efarkggtiditssidepvapaegiaravqagiplarvtlssdgngsqphigvagfetll etvqvlvkdydfsisdalrpltssvagflnltgkg
Timeline for d1onwb2: