![]() | 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 d1pokb2: 1pok B:63-346 [104210] Other proteins in same PDB: d1poka1, d1pokb1 complexed with asn, so4, zn |
PDB Entry: 1pok (more details), 2.7 Å
SCOPe Domain Sequences for d1pokb2:
Sequence, based on SEQRES records: (download)
>d1pokb2 c.1.9.13 (B:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli [TaxId: 562]} gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal efarkggtiditssidepvapaegiaravqagiplarvtlssdgngsqpffddegnlthi gvagfetlletvqvlvkdydfsisdalrpltssvagflnltgkg
>d1pokb2 c.1.9.13 (B:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli [TaxId: 562]} gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal efarkggtiditssidepvapaegiaravqagiplarvtlssdgngsvagfetlletvqv lvkdydfsisdalrpltssvagflnltgkg
Timeline for d1pokb2: