![]() | Class c: Alpha and beta proteins (a/b) [51349] (147 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] (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 |
![]() | Family c.36.1.6: TK-like Pyr module [88735] (2 proteins) different order of the modules, PP module is N-terminal, Pyr module is next to it followed by a Rossmann-like domain |
![]() | Protein Pyruvate dehydrogenase E1 component, Pyr module [88739] (1 species) E1A and E1B fused together in a single-chain protein |
![]() | Species Escherichia coli [TaxId:562] [88740] (8 PDB entries) |
![]() | Domain d2qtcb1: 2qtc B:471-700 [151346] Other proteins in same PDB: d2qtca2, d2qtca3, d2qtcb2, d2qtcb3 automatically matched to d1l8aa2 complexed with mg, tdk; mutant |
PDB Entry: 2qtc (more details), 1.77 Å
SCOPe Domain Sequences for d2qtcb1:
Sequence, based on SEQRES records: (download)
>d2qtcb1 c.36.1.6 (B:471-700) Pyruvate dehydrogenase E1 component, Pyr module {Escherichia coli [TaxId: 562]} eklelpslqdfgalleeqskeisttiafvralnvmlknksikdrlvpiiadeartfgmeg lfrqigiyspngqqytpqdreqvayykedekgqilqeginelgagcswlaaatsystnnl pmipfyiyysmfgfqrigdlcwaagdqqargfliggtsgrttlngeglqhedghshiqsl tipncisydpayayevavimhdglermygekqenvyyyittlnenyhmpa
>d2qtcb1 c.36.1.6 (B:471-700) Pyruvate dehydrogenase E1 component, Pyr module {Escherichia coli [TaxId: 562]} eklelpslqdfgalleeqskeisttiafvralnvmlknksikdrlvpiiadeartfgmeg lfrqigiyspedekgqilqeginelgagcswlaaatsystnnlpmipfyiyysmfgfqri gdlcwaagdqqargfliggtsgrttlngeglqhedghshiqsltipncisydpayayeva vimhdglermygekqenvyyyittlnenyhmpa
Timeline for d2qtcb1: