SCOPe 2.08: Domain d2cwna1: 2cwn A:13-331

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

1. Root: SCOPe 2.08

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

3. Fold 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. 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 Transaldolase [51588] (3 species)
   probably related to class I aldolases by a circular permutation

7. Species Mouse (Mus musculus) [TaxId:10090] [141835] (1 PDB entry)
   Uniprot Q93092 13-331

8. Domain 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, 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:

>d2cwna1 c.1.10.1 (A:13-331) Transaldolase {Mouse (Mus musculus) [TaxId: 10090]}
saldqlkqfttvvadtgdfnaideykpqdattnpslilaaaqmpayqelveeaiaygkkl
ggpqeeqiknaidklfvlfgaeilkkipgrvstevdarlsfdkdamvararrlielykea
gvgkdriliklsstwegiqagkeleeqhgihcnmtllfsfaqavacaeagvtlispfvgr
ildwhvantdkksyepqgdpgvksvtkiynyykkfgyktivmgasfrntgeikalagcdf
ltispkllgellkdnsklapalsvkaaqtsdsekihldekafrwlhnedqmaveklsdgi
rkfaadaiklermltermf

Timeline for d2cwna1:

• d2cwna1 first appeared in SCOP 1.73
  
• d2cwna1 appears in SCOPe 2.07