Class c: Alpha and beta proteins (a/b) [51349] (134 folds) |
Fold c.2: NAD(P)-binding Rossmann-fold domains [51734] (1 superfamily) core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456 The nucleotide-binding modes of this and the next two folds/superfamilies are similar |
Superfamily c.2.1: NAD(P)-binding Rossmann-fold domains [51735] (12 families) |
Family c.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain [51883] (11 proteins) extra N-terminal helix displaces the C-terminal helix (following strand 6) from its usual position creating a family nicotineamide-binding site |
Protein Methylenetetrahydrofolate dehydrogenase/cyclohydrolase [51894] (3 species) the two-domain organization is similar to that of aminoacid dehydrogenases, but both domains are truncated |
Species Human (Homo sapiens) [TaxId:9606] [51895] (4 PDB entries) |
Domain d1diba1: 1dib A:127-296 [30284] Other proteins in same PDB: d1diba2, d1dibb2 |
PDB Entry: 1dib (more details), 2.7 Å
SCOP Domain Sequences for d1diba1:
Sequence, based on SEQRES records: (download)
>d1diba1 c.2.1.7 (A:127-296) Methylenetetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)} ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginyvpddkk pngrkvvgdvaydeakerasfitpvpggvgpmtvamlmqstvesakrfle
>d1diba1 c.2.1.7 (A:127-296) Methylenetetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens)} ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginykvvgdv aydeakerasfitpvpggvgpmtvamlmqstvesakrfle
Timeline for d1diba1: