SCOPe 2.06: Domain d5hhta1: 5hht A:2-332

Lineage for d5hhta1 (5hht A:2-332)

1. Root: SCOPe 2.06

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

3. Fold c.36: Thiamin diphosphate-binding fold (THDP-binding) [52517] (1 superfamily)
   3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465

4. Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (9 families)
   there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules
   two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules

5. Family c.36.1.10: TK-like PP module [88760] (3 proteins)
   different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain

6. Protein automated matches [254698] (2 species)
   not a true protein

7. Species Escherichia coli [TaxId:83333] [324638] (1 PDB entry)

8. Domain d5hhta1: 5hht A:2-332 [324668]
   Other proteins in same PDB: d5hhta2, d5hhta3, d5hhtb2, d5hhtb3, d5hhtb4
   automated match to d1qgda2
   complexed with ca, edo, tdp

Details for d5hhta1

PDB Entry: 5hht, 1.5 Å

PDB Description: crystal structure of e. coli transketolase triple variant ser385tyr/asp469thr/arg520gln

PDB Compounds: (A:) Transketolase 1

SCOPe Domain Sequences for d5hhta1:

Sequence; same for both SEQRES and ATOM records:

>d5hhta1 c.36.1.10 (A:2-332) automated matches {Escherichia coli [TaxId: 83333]}
ssrkelanairalsmdavqkaksghpgapmgmadiaevlwrdflkhnpqnpswadrdrfv
lsnghgsmliysllhltgydlpmeelknfrqlhsktpghpevgytagvetttgplgqgia
navgmaiaektlaaqfnrpghdivdhytyafmgdgcmmegishevcslagtlklgkliaf
yddngisidghvegwftddtamrfeaygwhvirdidghdaasikraveearavtdkpsll
mcktiigfgspnkagthdshgaplgdaeialtreqlgwkyapfeipseiyaqwdakeagq
akesawnekfaayakaypqeaaeftrrmkge

Timeline for d5hhta1:

• d5hhta1 is new in SCOPe 2.06-stable
  
• d5hhta1 appears in SCOPe 2.07
  
• d5hhta1 appears in the current release, SCOPe 2.08