Lineage for d1nhsa1 (1nhs A:1-119,A:243-321)

  1. Root: SCOPe 2.06
  2. 2078559Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2096453Fold c.3: FAD/NAD(P)-binding domain [51904] (1 superfamily)
    core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander
  4. 2096454Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families) (S)
  5. 2096984Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (15 protein domains)
    duplication: both domains have similar folds and functions
    most members of the family contain common C-terminal alpha+beta domain
  6. 2097162Protein NADH peroxidase [51955] (1 species)
  7. 2097163Species Enterococcus faecalis [TaxId:1351] [51956] (8 PDB entries)
  8. 2097164Domain d1nhsa1: 1nhs A:1-119,A:243-321 [30555]
    Other proteins in same PDB: d1nhsa3
    complexed with fad, so4; mutant

Details for d1nhsa1

PDB Entry: 1nhs (more details), 2 Å

PDB Description: an l40c mutation converts the cysteine-sulfenic acid redox centre in enterococcal nadh peroxidase to a disulfide
PDB Compounds: (A:) nadh peroxidase

SCOPe Domain Sequences for d1nhsa1:

Sequence; same for both SEQRES and ATOM records: (download)

>d1nhsa1 c.3.1.5 (A:1-119,A:243-321) NADH peroxidase {Enterococcus faecalis [TaxId: 1351]}

SCOPe Domain Coordinates for d1nhsa1:

Click to download the PDB-style file with coordinates for d1nhsa1.
(The format of our PDB-style files is described here.)

Timeline for d1nhsa1: