Structural Classification of Proteins
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Protein: NADH peroxidase from Enterococcus faecalis [TaxId: 1351]

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b) [51349]
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: FAD/NAD(P)-binding domain [51904]
    core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander
  4. Superfamily: FAD/NAD(P)-binding domain [51905]
    link to SUPERFAMILY database - Superfamily
  5. Family: FAD/NAD-linked reductases, N-terminal and central domains [51943]
    duplication: both domains have similar folds and functions
    most members of the family contain common C-terminal alpha+beta domain
  6. Protein: NADH peroxidase [51955]
  7. Species: Enterococcus faecalis [TaxId: 1351] [51956]

PDB Entry Domains:

  1. 1nhp picpicxref
    complexed with fad, so4; mutant
    1. region a:1-119,a:243-321 [30549] picpiclink
    2. region a:120-242 [30550] picpiclink
  2. 1nhs picpicxref
    complexed with cyo, fad, so4; mutant
    1. region a:1-119,a:243-321 [30555] picpiclink
    2. region a:120-242 [30556] picpiclink
  3. 1nhq picpicxref
    complexed with fad, so4; mutant
    1. region a:1-119,a:243-321 [30551] picpiclink
    2. region a:120-242 [30552] picpiclink
  4. 1nhr picpicxref
    complexed with fad, so4; mutant
    1. region a:1-119,a:243-321 [30553] picpiclink
    2. region a:120-242 [30554] picpiclink
  5. 1npx picpicxref
    complexed with cyo, fad
    1. region a:1-119,a:243-321 [30557] picpiclink
    2. region a:120-242 [30558] picpiclink
  6. 2npx picpicxref
    complexed with cyo, fad, nad
    1. region a:1-119,a:243-321 [30559] picpiclink
    2. region a:120-242 [30560] picpiclink
  7. 1f8w picpicxref
    complexed with fad; mutant
    1. region a:1-119,a:243-321 [30561] picpiclink
    2. region a:120-242 [30562] picpiclink
  8. 1joa picpicxref
    complexed with fad
    1. region a:1-119,a:243-321 [30563] picpiclink
    2. region a:120-242 [30564] picpiclink
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MRC site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk