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 d2ieab1: 2iea B:471-700 [137297] Other proteins in same PDB: d2ieaa2, d2ieaa3, d2ieab2, d2ieab3 automatically matched to d1l8aa2 complexed with mg, tdp |
PDB Entry: 2iea (more details), 1.85 Å
SCOP Domain Sequences for d2ieab1:
Sequence, based on SEQRES records: (download)
>d2ieab1 c.36.1.6 (B:471-700) Pyruvate dehydrogenase E1 component, Pyr module {Escherichia coli [TaxId: 562]} eklelpslqdfgalleeqskeisttiafvralnvmlknksikdrlvpiiadeartfgmeg lfrqigiyspngqqytpqdreqvayykedekgqilqeginelgagcswlaaatsystnnl pmipfyiyysmfgfqrigdlcwaagdqqargfliggtsgrttlngeglqhedghshiqsl tipncisydpayayevavimhdglermygekqenvyyyittlnenyhmpa
>d2ieab1 c.36.1.6 (B:471-700) Pyruvate dehydrogenase E1 component, Pyr module {Escherichia coli [TaxId: 562]} eklelpslqdfgalleeqskeisttiafvralnvmlknksikdrlvpiiadeartfgmeg lfrqigiyspedekgqilqeginelgagcswlaaatsystnnlpmipfyiyysmfgfqri gdlcwaagdqqargfliggtsgrttlngeglqhedghshiqsltipncisydpayayeva vimhdglermygekqenvyyyittlnenyhmpa
Timeline for d2ieab1: