Lineage for d2wnqa1 (2wnq A:2-297)

  1. Root: SCOPe 2.06
  2. 2078559Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2078560Fold 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. 2085156Superfamily c.1.10: Aldolase [51569] (9 families) (S)
    Common fold covers whole protein structure
  5. 2085157Family c.1.10.1: Class I aldolase [51570] (13 protein domains)
    the catalytic lysine forms schiff-base intermediate with substrate
    possible link between the aldolase superfamily and the phosphate-binding beta/alpha barrels
  6. 2085665Protein automated matches [190095] (24 species)
    not a true protein
  7. 2085733Species Escherichia coli [TaxId:562] [189174] (7 PDB entries)
  8. 2085746Domain d2wnqa1: 2wnq A:2-297 [169482]
    Other proteins in same PDB: d2wnqa2, d2wnqc2, d2wnqd2
    automated match to d1hl2a_
    complexed with cl; mutant

Details for d2wnqa1

PDB Entry: 2wnq (more details), 1.8 Å

PDB Description: structure of the e192n mutant of e. coli n-acetylneuraminic acid lyase in space group p21
PDB Compounds: (A:) n-acetylneuraminate lyase

SCOPe Domain Sequences for d2wnqa1:

Sequence; same for both SEQRES and ATOM records: (download)

>d2wnqa1 c.1.10.1 (A:2-297) automated matches {Escherichia coli [TaxId: 562]}

SCOPe Domain Coordinates for d2wnqa1:

Click to download the PDB-style file with coordinates for d2wnqa1.
(The format of our PDB-style files is described here.)

Timeline for d2wnqa1: