SCOPe 2.06: Domain d5lnxd1: 5lnx D:1-226

Lineage for d5lnxd1 (5lnx D:1-226)

1. Root: SCOPe 2.06

2. Class e: Multi-domain proteins (alpha and beta) [56572] (69 folds)

3. Fold e.6: Acyl-CoA dehydrogenase NM domain-like [56644] (1 superfamily)
   2 domains: (1) all-alpha: 5 helices; (2) contains an open beta-sheet barrel: n*=5, S*=8; complex topology

4. Superfamily e.6.1: Acyl-CoA dehydrogenase NM domain-like [56645] (3 families)
   flavoprotein: binds FAD; constituent families differ in the numbers of C-terminal domains (four-helical bundles)

5. Family e.6.1.0: automated matches [227203] (1 protein)
   not a true family

6. Protein automated matches [226934] (25 species)
   not a true protein

7. Species Bacillus subtilis [TaxId:224308] [337846] (1 PDB entry)

8. Domain d5lnxd1: 5lnx D:1-226 [337849]
   Other proteins in same PDB: d5lnxa2, d5lnxb2, d5lnxc2, d5lnxd2, d5lnxe2, d5lnxf2, d5lnxg2, d5lnxh2
   automated match to d3mdea2
   complexed with fad, gol

Details for d5lnxd1

PDB Entry: 5lnx, 2.6 Å

PDB Description: crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.

PDB Compounds: (D:) acyl-CoA dehydrogenase

SCOPe Domain Sequences for d5lnxd1:

Sequence, based on SEQRES records:

>d5lnxd1 e.6.1.0 (D:1-226) automated matches {Bacillus subtilis [TaxId: 224308]}
mhvtqeqvmmrkmvrdfarkeiapaaeimektdefpfqlikkmgkhglmgipvpeqygga
gadvvsyilaiheisrisaavgvilsvhtsvgtnpilyfgneeqkmkyipnlasgdhlga
faltephsgsdagslrttaikkngkyllngskifitnggaadiyitfaltapdqgrhgis
afivekntpgftvgkkerklglygsnttelifdnaevpeanllgke

Sequence, based on observed residues (ATOM records):

>d5lnxd1 e.6.1.0 (D:1-226) automated matches {Bacillus subtilis [TaxId: 224308]}
mhvqeqvmmrkmvrdfarkeiapaaeimektdefpfqlikkmgkhglmgipvpeqyggag
advvsyilaiheisrisaavgvilsvhtsvgtnpilyfgneeqkmkyipnlasgdhlgaf
altephsgsdagslrttaikkngkyllngskifitnggaadiyitfaltapdqgrhgisa
fivekntpgftvgkkerklglygsnttelifdnaevpeanllgke

Timeline for d5lnxd1:

• d5lnxd1 is new in SCOPe 2.06-stable
  
• d5lnxd1 appears in SCOPe 2.07
  
• d5lnxd1 appears in the current release, SCOPe 2.08