![]() | 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 Mitochondrial NAD(P)-dependent malic enzyme [51898] (3 species) includes C-terminal additional subdomains |
![]() | Species Human (Homo sapiens) [TaxId:9606] [51899] (10 PDB entries) |
![]() | Domain d1efla1: 1efl A:280-573 [30295] Other proteins in same PDB: d1efla2, d1eflb2, d1eflc2, d1efld2 complexed with mg, nad, ttn has additional subdomain(s) that are not in the common domain |
PDB Entry: 1efl (more details), 2.6 Å
SCOPe Domain Sequences for d1efla1:
Sequence; same for both SEQRES and ATOM records: (download)
>d1efla1 c.2.1.7 (A:280-573) Mitochondrial NAD(P)-dependent malic enzyme {Human (Homo sapiens) [TaxId: 9606]} iqgtaavalagllaaqkviskpisehkilflgageaalgianlivmsmvenglseqeaqk kiwmfdkygllvkgrkakidsyqepfthsapesipdtfedavnilkpstiigvagagrlf tpdviramasinerpvifalsnptaqaectaeeaytltegrclfasgspfgpvkltdgrv ftpgqgnnvyifpgvalavilcntrhisdsvfleaakaltsqltdeelaqgrlypplani qevsiniaikvteylyankmafrypepedkakyvkertwrseydsllpdvyewp
Timeline for d1efla1: