Class c: Alpha and beta proteins (a/b) [51349] (141 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.36.1.10: 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 |
Protein Pyruvate dehydrogenase E1 component, PP module [88764] (1 species) E1A and E1B fused together in a single-chain protein |
Species Escherichia coli [TaxId:562] [88765] (6 PDB entries) |
Domain d2g25b2: 2g25 B:56-470 [134527] Other proteins in same PDB: d2g25a1, d2g25a3, d2g25b1, d2g25b3 automatically matched to d1l8aa1 complexed with mg, po4, tdk |
PDB Entry: 2g25 (more details), 2.1 Å
SCOP Domain Sequences for d2g25b2:
Sequence; same for both SEQRES and ATOM records: (download)
>d2g25b2 c.36.1.10 (B:56-470) Pyruvate dehydrogenase E1 component, PP module {Escherichia coli [TaxId: 562]} isnyintipveeqpeypgnlelerrirsairwnaimtvlraskkdlelgghmasfqssat iydvcfnhffrarneqdggdlvyfqghispgvyaraflegrltqeqldnfrqevhgngls syphpklmpefwqfptvsmglgpigaiyqakflkylehrglkdtskqtvyaflgdgemde peskgaitiatrekldnlvfvincnlqrldgpvtgngkiinelegifegagwnvikvmwg srwdellrkdtsgkliqlmnetvdgdyqtfkskdgayvrehffgkypetaalvadwtdeq iwalnrgghdpkkiyaafkkaqetkgkatvilahtikgygmgdaaegkniahqvkkmnmd gvrhirdrfnvpvsdadieklpyitfpegseehtylhaqrqklhgylpsrqpnft
Timeline for d2g25b2: