![]() | Class c: Alpha and beta proteins (a/b) [51349] (148 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] (13 families) ![]() |
![]() | Family c.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain [51883] (12 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] (7 PDB entries) |
![]() | Domain d6ecrb2: 6ecr B:127-296 [366748] Other proteins in same PDB: d6ecra1, d6ecrb1 automated match to d1a4ia1 complexed with act, nap missing some secondary structures that made up less than one-third of the common domain |
PDB Entry: 6ecr (more details), 2.2 Å
SCOPe Domain Sequences for d6ecrb2:
Sequence; same for both SEQRES and ATOM records: (download)
>d6ecrb2 c.2.1.7 (B:127-296) Methylenetetrahydrofolate dehydrogenase/cyclohydrolase {Human (Homo sapiens) [TaxId: 9606]} ltsinagrlargdlndcfipctpkgcleliketgvpiagrhavvvgrskivgapmhdlll wnnatvttchsktahldeevnkgdilvvatgqpemvkgewikpgaividcginyvpddkk pngrkvvgdvaydeakerasfitpvpggvgpmtvamlmqstvesakrfle
Timeline for d6ecrb2: