![]() | Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
![]() | 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 |
![]() | 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 |
![]() | 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 |
![]() | Protein Transketolase (TK), PP module [88761] (4 species) |
![]() | Species Escherichia coli [TaxId:562] [89656] (4 PDB entries) |
![]() | Domain d2r5na2: 2r5n A:2-332 [151592] Other proteins in same PDB: d2r5na1, d2r5na3, d2r5na4, d2r5nb1, d2r5nb3, d2r5nb4 automated match to d1qgda2 complexed with ca, edo, r5p, rp5, tpp |
PDB Entry: 2r5n (more details), 1.6 Å
SCOPe Domain Sequences for d2r5na2:
Sequence; same for both SEQRES and ATOM records: (download)
>d2r5na2 c.36.1.10 (A:2-332) Transketolase (TK), PP module {Escherichia coli [TaxId: 562]} ssrkelanairalsmdavqkaksghpgapmgmadiaevlwrdflkhnpqnpswadrdrfv lsnghgsmliysllhltgydlpmeelknfrqlhsktpghpevgytagvetttgplgqgia navgmaiaektlaaqfnrpghdivdhytyafmgdgcmmegishevcslagtlklgkliaf yddngisidghvegwftddtamrfeaygwhvirdidghdaasikraveearavtdkpsll mcktiigfgspnkagthdshgaplgdaeialtreqlgwkyapfeipseiyaqwdakeagq akesawnekfaayakaypqeaaeftrrmkge
Timeline for d2r5na2:
![]() Domains from other chains: (mouse over for more information) d2r5nb1, d2r5nb2, d2r5nb3, d2r5nb4 |