SCOPe 2.06: Domain d1onxa2: 1onx A:63-346

Lineage for d1onxa2 (1onx A:63-346)

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. 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

4. 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

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)
   Uniprot P39377

8. Domain d1onxa2: 1onx A:63-346 [87177]
   Other proteins in same PDB: d1onxa1, d1onxb1
   complexed with asp, zn

Details for d1onxa2

PDB Entry: 1onx, 2.1 Å

PDB Description: crystal structure of isoaspartyl dipeptidase from escherichia coli complexed with aspartate

PDB Compounds: (A:) Isoaspartyl dipeptidase

SCOPe Domain Sequences for d1onxa2:

Sequence; same for both SEQRES and ATOM records:

>d1onxa2 c.1.9.13 (A:63-346) Isoaspartyl dipeptidase, catalytic domain {Escherichia coli [TaxId: 562]}
gfidqhvhliggggeagpttrtpevalsrlteagvtsvvgllgtdsisrhpesllaktra
lneegisawmltgayhvpsrtitgsvekdvaiidrvigvkcaisdhrsaapdvyhlanma
aesrvggllggkpgvtvfhmgdskkalqpiydllencdvpiskllpthvnrnvplfeqal
efarkggtiditssidepvapaegiaravqagiplarvtlssdgngsqpffddegnlthi
gvagfetlletvqvlvkdydfsisdalrpltssvagflnltgkg

Timeline for d1onxa2:

• d1onxa2 first appeared in SCOP 1.65
  
• d1onxa2 appears in SCOPe 2.05
  
• d1onxa2 appears in SCOPe 2.07
  
• d1onxa2 appears in the current release, SCOPe 2.08