SCOP 1.69: Domain d1po9a2: 1po9 A:63-346

Lineage for d1po9a2 (1po9 A:63-346)

1. Root: SCOP 1.69

2. Class c: Alpha and beta proteins (a/b) [51349] (136 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (31 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] (13 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.1.9.13: Isoaspartyl dipeptidase, catalytic domain [89489] (1 protein)

6. Protein Isoaspartyl dipeptidase, catalytic domain [89490] (1 species)

7. Species Escherichia coli [TaxId:562] [89491] (5 PDB entries)

8. Domain d1po9a2: 1po9 A:63-346 [104200]
   Other proteins in same PDB: d1po9a1, d1po9b1

Details for d1po9a2

PDB Entry: 1po9, 2 Å

PDB Description: Crytsal structure of isoaspartyl dipeptidase

SCOP Domain Sequences for d1po9a2:

Sequence, based on SEQRES records:

>d1po9a2 c.1.9.13 (A:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli}
gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra
lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma
aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal
efarkggtiditssidepvapaegiaravqagiplarvtlssdgngsqpffddegnlthi
gvagfetlletvqvlvkdydfsisdalrpltssvagflnltgkg

Sequence, based on observed residues (ATOM records):

>d1po9a2 c.1.9.13 (A:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli}
gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra
lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma
aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal
efarkggtiditssidepvapaegiaravqagiplarvtlssdgngvagfetlletvqvl
vkdydfsisdalrpltssvagflnltgkg

Timeline for d1po9a2:

• d1po9a2 is new in SCOP 1.69
  
• d1po9a2 appears in SCOP 1.71
  
• d1po9a2 appears in the current release, SCOPe 2.08