SCOPe 2.03: Domain d1dpma_: 1dpm A:

Lineage for d1dpma_ (1dpm A:)

1. Root: SCOPe 2.03

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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.1.9.3: Phosphotriesterase-like [51564] (3 proteins)
   automatically mapped to Pfam PF02126

6. Protein Phosphotriesterase (parathion hydrolase, PTE) [51565] (4 species)

7. Species Pseudomonas diminuta [TaxId:293] [51566] (19 PDB entries)
   Uniprot P0A434 30-365

8. Domain d1dpma_: 1dpm A: [29062]
   complexed with ebp, fmt, zn

Details for d1dpma_

PDB Entry: 1dpm, 2.1 Å

PDB Description: three-dimensional structure of the zinc-containing phosphotriesterase with bound substrate analog diethyl 4-methylbenzylphosphonate

PDB Compounds: (A:) phosphotriesterase

SCOPe Domain Sequences for d1dpma_:

Sequence; same for both SEQRES and ATOM records:

>d1dpma_ c.1.9.3 (A:) Phosphotriesterase (parathion hydrolase, PTE) {Pseudomonas diminuta [TaxId: 293]}
arintvrgpitiseagftlthehicgssagflrawpeffgsrkalaekavrglrraraag
vrtivdvstfdigrdvsllaevsraadvhivaatglwfdpplsmrlrsveeltqfflrei
qygiedtgiragiikvattgkatpfqelvlkaaaraslatgvpvtthtaasqrdgeqqaa
ifeseglspsrvcighsddtddlsyltalaargyligldhiphsaiglednasasallgi
rswqtrallikalidqgymkqilvsndwlfgfssyvtnimdvmdrvnpdgmafiplrvip
flrekgvpqetlagitvtnparflsptlr

Timeline for d1dpma_:

• d1dpma_ first appeared (with stable ids) in SCOP 1.55
  
• d1dpma_ appears in SCOPe 2.02
  
• d1dpma_ appears in SCOPe 2.04
  
• d1dpma_ appears in the current release, SCOPe 2.08