SCOP 1.69: Domain d1tkka1: 1tkk A:126-358

Lineage for d1tkka1 (1tkk A:126-358)

1. Root: SCOP 1.69

2. Class c: Alpha and beta proteins (a/b) [51349] (136 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (31 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.1.11: Enolase C-terminal domain-like [51604] (2 families)
   binds metal ion (magnesium or manganese) in conserved site inside barrel
   N-terminal alpha+beta domain is common to this family

5. Family c.1.11.2: D-glucarate dehydratase-like [51609] (9 proteins)

6. Protein L-Ala-D/L-Glu epimerase [69397] (2 species)

7. Species Bacillus subtilis [TaxId:1423] [69399] (2 PDB entries)

8. Domain d1tkka1: 1tkk A:126-358 [107089]
   Other proteins in same PDB: d1tkka2, d1tkkb2, d1tkkc2, d1tkkd2, d1tkke2, d1tkkf2, d1tkkg2, d1tkkh2

Details for d1tkka1

PDB Entry: 1tkk, 2.1 Å

PDB Description: The Structure of a Substrate-Liganded Complex of the L-Ala-D/L-Glu Epimerase from Bacillus subtilis

SCOP Domain Sequences for d1tkka1:

Sequence; same for both SEQRES and ATOM records:

>d1tkka1 c.1.11.2 (A:126-358) L-Ala-D/L-Glu epimerase {Bacillus subtilis}
yrdtletdytvsvnspeemaadaenylkqgfqtlkikvgkddiatdiariqeirkrvgsa
vklrldanqgwrpkeavtairkmedaglgielveqpvhkddlaglkkvtdatdtpimade
svftprqafevlqtrsadliniklmkaggisgaekinamaeacgvecmvgsmietklgit
aaahfaaskrnitrfdfdaplmlktdvfnggitysgstismpgkpglgiigaa

Timeline for d1tkka1:

• d1tkka1 is new in SCOP 1.69
  
• d1tkka1 appears in SCOP 1.71
  
• d1tkka1 appears in the current release, SCOPe 2.08