Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
Fold c.1: TIM beta/alpha-barrel [51350] (34 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.1.9.13: Isoaspartyl dipeptidase, catalytic domain [89489] (1 protein) |
Protein Isoaspartyl dipeptidase, catalytic domain [89490] (1 species) |
Species Escherichia coli [TaxId:562] [89491] (5 PDB entries) Uniprot P39377 |
Domain d1po9a2: 1po9 A:63-346 [104200] Other proteins in same PDB: d1po9a1, d1po9b1 complexed with zn |
PDB Entry: 1po9 (more details), 2 Å
SCOPe Domain Sequences for d1po9a2:
Sequence, based on SEQRES records: (download)
>d1po9a2 c.1.9.13 (A:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli [TaxId: 562]} gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal efarkggtiditssidepvapaegiaravqagiplarvtlssdgngsqpffddegnlthi gvagfetlletvqvlvkdydfsisdalrpltssvagflnltgkg
>d1po9a2 c.1.9.13 (A:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli [TaxId: 562]} gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal efarkggtiditssidepvapaegiaravqagiplarvtlssdgngvagfetlletvqvl vkdydfsisdalrpltssvagflnltgkg
Timeline for d1po9a2: