SCOP 1.73: Domain d1c0la1: 1c0l A:999-1193,A:1289-1361

Lineage for d1c0la1 (1c0l A:999-1193,A:1289-1361)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 folds)

3. Fold c.4: Nucleotide-binding domain [51970] (1 superfamily)
   3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32145; Rossmann-like

4. Superfamily c.4.1: Nucleotide-binding domain [51971] (3 families)
   this superfamily shares the common nucleotide-binding site with and provides a link between the Rossmann-fold NAD(P)-binding and FAD/NAD(P)-binding domains

5. Family c.4.1.2: D-aminoacid oxidase, N-terminal domain [51979] (1 protein)
   This family is probably related to the FAD-linked reductases and shares with them the C-terminal domain fold

6. Protein D-aminoacid oxidase, N-terminal domain [51980] (2 species)

7. Species Rhodotorula gracilis [TaxId:5286] [51982] (4 PDB entries)

8. Domain d1c0la1: 1c0l A:999-1193,A:1289-1361 [30649]
   Other proteins in same PDB: d1c0la2
   complexed with fad

Details for d1c0la1

PDB Entry: 1c0l, 1.73 Å

PDB Description: d-amino acid oxidase: structure of substrate complexes at very high resolution reveal the chemical reacttion mechanism of flavin dehydrogenation

PDB Compounds: (A:) d-amino acid oxidase

SCOP Domain Sequences for d1c0la1:

Sequence; same for both SEQRES and ATOM records:

>d1c0la1 c.4.1.2 (A:999-1193,A:1289-1361) D-aminoacid oxidase, N-terminal domain {Rhodotorula gracilis [TaxId: 5286]}
lmmhsqkrvvvlgsgviglssalilarkgysvhilardlpedvssqtfaspwaganwtpf
mtltdgprqakweestfkkwvelvptghamwlkgtrrfaqnedgllghwykditpnyrpl
pssecppgaigvtydtlsvhapkycqylarelqklgatferrtvtsleqafdgadlvvna
tglgaksiagiddqaXrggprveaerivlpldrtksplslgrgsaraakekevtlvhayg
fssagyqqswgaaedvaqlvdeafqryhg

Timeline for d1c0la1:

• d1c0la1 first appeared (with stable ids) in SCOP 1.55
  
• d1c0la1 appears in SCOP 1.71
  
• d1c0la1 appears in SCOP 1.75
  
• d1c0la1 appears in the current release, SCOPe 2.08