SCOPe 2.06: Domain d2xfwa1: 2xfw A:2-297

Lineage for d2xfwa1 (2xfw A:2-297)

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.1.10: Aldolase [51569] (9 families)
   Common fold covers whole protein structure

5. Family c.1.10.1: Class I aldolase [51570] (13 proteins)
   the catalytic lysine forms schiff-base intermediate with substrate
   possible link between the aldolase superfamily and the phosphate-binding beta/alpha barrels

6. Protein automated matches [190095] (24 species)
   not a true protein

7. Species Escherichia coli [TaxId:469008] [189446] (6 PDB entries)

8. Domain d2xfwa1: 2xfw A:2-297 [207206]
   Other proteins in same PDB: d2xfwa2, d2xfwb2, d2xfwc2, d2xfwd2
   automated match to d2wnzd_
   complexed with 1pe, pyr; mutant

Details for d2xfwa1

PDB Entry: 2xfw, 1.65 Å

PDB Description: Structure of the E192N mutant of E. coli N-acetylneuraminic acid lyase in complex with pyruvate in crystal form III

PDB Compounds: (A:) n-acetylneuraminic acid lyase

SCOPe Domain Sequences for d2xfwa1:

Sequence; same for both SEQRES and ATOM records:

>d2xfwa1 c.1.10.1 (A:2-297) automated matches {Escherichia coli [TaxId: 469008]}
atnlrgvmaalltpfdqqqaldkaslrrlvqfniqqgidglyvggstgeafvqslsereq
vleivaeeakgkikliahvgcvstaesqqlaasakrygfdavsavtpfyypfsfeehcdh
yraiidsadglpmvvynipalsgvkltldqintlvtlpgvgalxqtsgdlyqmeqirreh
pdlvlyngydnifasgllagadggigstynimgwryqgivkalkegdiqtaqklqtecnk
vidlliktgvfrglktvlhymdvvsvplcrkpfgpvdekylpelkalaqqlmqerg

Timeline for d2xfwa1:

• d2xfwa1 first appeared in SCOPe 2.03, called d2xfwa_
  
• d2xfwa1 was called d2xfwa_ in SCOPe 2.05
  
• d2xfwa1 appears in SCOPe 2.07
  
• d2xfwa1 appears in the current release, SCOPe 2.08