Lineage for d2cwna1 (2cwn A:13-331)

  1. Root: SCOPe 2.08
  2. 2826024Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2826025Fold c.1: TIM beta/alpha-barrel [51350] (34 superfamilies)
    contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
    the first seven superfamilies have similar phosphate-binding sites
  4. 2834402Superfamily c.1.10: Aldolase [51569] (9 families) (S)
    Common fold covers whole protein structure
  5. 2834403Family 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. 2834930Protein Transaldolase [51588] (3 species)
    probably related to class I aldolases by a circular permutation
  7. 2834949Species Mouse (Mus musculus) [TaxId:10090] [141835] (1 PDB entry)
    Uniprot Q93092 13-331
  8. 2834950Domain d2cwna1: 2cwn A:13-331 [130929]
    Other proteins in same PDB: d2cwna2, d2cwnb_
    has additional insertions and/or extensions that are not grouped together

Details for d2cwna1

PDB Entry: 2cwn (more details), 2.1 Å

PDB Description: crystal structure of mouse transaldolase
PDB Compounds: (A:) Transaldolase

SCOPe Domain Sequences for d2cwna1:

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

>d2cwna1 c.1.10.1 (A:13-331) Transaldolase {Mouse (Mus musculus) [TaxId: 10090]}

SCOPe Domain Coordinates for d2cwna1:

Click to download the PDB-style file with coordinates for d2cwna1.
(The format of our PDB-style files is described here.)

Timeline for d2cwna1:

View in 3D
Domains from same chain:
(mouse over for more information)
View in 3D
Domains from other chains:
(mouse over for more information)