SCOP 1.65: Domain d1l1ff1: 1l1f F:213-505

Lineage for d1l1ff1 (1l1f F:213-505)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 folds)

3. 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

4. Superfamily c.2.1: NAD(P)-binding Rossmann-fold domains [51735] (10 families)

5. Family c.2.1.7: Aminoacid dehydrogenase-like, C-terminal domain [51883] (10 proteins)
   extra N-terminal helix displaces the C-terminal helix (following strand 6) from its usual position creating a family nicotineamide-binding site

6. Protein Glutamate dehydrogenase [51884] (7 species)

7. Species Human (Homo sapiens) [TaxId:9606] [75115] (2 PDB entries)

8. Domain d1l1ff1: 1l1f F:213-505 [73466]
   Other proteins in same PDB: d1l1fa2, d1l1fb2, d1l1fc2, d1l1fd2, d1l1fe2, d1l1ff2

Details for d1l1ff1

PDB Entry: 1l1f, 2.7 Å

PDB Description: Structure of human glutamate dehydrogenase-apo form

SCOP Domain Sequences for d1l1ff1:

Sequence; same for both SEQRES and ATOM records:

>d1l1ff1 c.2.1.7 (F:213-505) Glutamate dehydrogenase {Human (Homo sapiens)}
hgrisatgrgvfhgienfineasymsilgmtpgfgdktfvvqgfgnvglhsmrylhrfga
kciavgesdgsiwnpdgidpkeledfklqhgsilgfpkakpyegsileadcdilipaase
kqltksnaprvkakiiaegangpttpeadkiflernimvipdlylnaggvtvsyfewlkn
lnhvsygrltfkyerdsnyhllmsvqeslerkfgkhggtipivptaefqdrisgasekdi
vhsglaytmersarqimrtamkynlgldlrtaayvnaiekvfkvyneagvtft

Timeline for d1l1ff1:

• d1l1ff1 first appeared in SCOP 1.61
  
• d1l1ff1 appears in SCOP 1.63
  
• d1l1ff1 appears in SCOP 1.67
  
• d1l1ff1 appears in the current release, SCOPe 2.08