SCOP 1.75: Domain d2r5nb2: 2r5n B:2-332

Lineage for d2r5nb2 (2r5n B:2-332)

1. Root: SCOP 1.75

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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] (8 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] (2 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 Transketolase (TK), PP module [88761] (4 species)

7. Species Escherichia coli [TaxId:562] [89656] (4 PDB entries)

8. Domain d2r5nb2: 2r5n B:2-332 [151595]
   Other proteins in same PDB: d2r5na1, d2r5na3, d2r5nb1, d2r5nb3
   automatically matched to d1qgda2
   complexed with ca, edo, r5p, rp5, tpp

Details for d2r5nb2

PDB Entry: 2r5n, 1.6 Å

PDB Description: crystal structure of transketolase from escherichia coli in noncovalent complex with acceptor aldose ribose 5-phosphate

PDB Compounds: (B:) Transketolase 1

SCOP Domain Sequences for d2r5nb2:

Sequence; same for both SEQRES and ATOM records:

>d2r5nb2 c.36.1.10 (B:2-332) Transketolase (TK), PP module {Escherichia coli [TaxId: 562]}
ssrkelanairalsmdavqkaksghpgapmgmadiaevlwrdflkhnpqnpswadrdrfv
lsnghgsmliysllhltgydlpmeelknfrqlhsktpghpevgytagvetttgplgqgia
navgmaiaektlaaqfnrpghdivdhytyafmgdgcmmegishevcslagtlklgkliaf
yddngisidghvegwftddtamrfeaygwhvirdidghdaasikraveearavtdkpsll
mcktiigfgspnkagthdshgaplgdaeialtreqlgwkyapfeipseiyaqwdakeagq
akesawnekfaayakaypqeaaeftrrmkge

Timeline for d2r5nb2:

• d2r5nb2 is new in SCOP 1.75
  
• d2r5nb2 appears in SCOPe 2.01
  
• d2r5nb2 appears in the current release, SCOPe 2.08