![]() | Class d: Alpha and beta proteins (a+b) [53931] (396 folds) |
![]() | Fold d.81: FwdE/GAPDH domain-like [55346] (4 superfamilies) core: alpha-beta-alpha-beta(3); mixed sheet: 2134, strand 2 is parallel to strand 1 |
![]() | Superfamily d.81.1: Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain [55347] (5 families) ![]() N-terminal domain is the classic Rossmann-fold |
![]() | Family d.81.1.2: Homoserine dehydrogenase-like [55363] (2 proteins) |
![]() | Protein Saccharopine reductase [55366] (1 species) contains an alpha-helical subdomain inserted in the common fold and other additional secondary structures |
![]() | Species Fungus (Magnaporthe grisea) [TaxId:148305] [55367] (3 PDB entries) |
![]() | Domain d1e5qf2: 1e5q F:125-391 [39960] Other proteins in same PDB: d1e5qa1, d1e5qb1, d1e5qc1, d1e5qd1, d1e5qe1, d1e5qf1, d1e5qg1, d1e5qh1 complexed with ndp, shr |
PDB Entry: 1e5q (more details), 2.1 Å
SCOPe Domain Sequences for d1e5qf2:
Sequence; same for both SEQRES and ATOM records: (download)
>d1e5qf2 d.81.1.2 (F:125-391) Saccharopine reductase {Fungus (Magnaporthe grisea) [TaxId: 148305]} ldpgidhlyaiktieevhaaggkiktflsycgglpapessdnplgykfswssrgvllalr naasfykdgkvtnvagpelmatakpyfiypgfafvaypnrdstpykeryqipeadnivrg tlryqgfpqfikvlvdigflsdeeqpflkeaipwkeatqkivkassaseqdivstivsna tfesteeqkrivaglkwlgifsdkkitprgnaldtlcatleekmqfeegerdlvmlqhkf eienkdgsretrtsslceygapigsgg
Timeline for d1e5qf2: