SCOPe 2.08: Domain d1nhsa1: 1nhs A:1-119,A:243-321

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

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold 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. Superfamily c.3.1: FAD/NAD(P)-binding domain [51905] (9 families)

5. Family c.3.1.5: FAD/NAD-linked reductases, N-terminal and central domains [51943] (25 proteins)
   duplication: both domains have similar folds and functions
   most members of the family contain common C-terminal alpha+beta domain

6. Protein NADH peroxidase, N- and C-terminal domain [418946] (1 species)

7. Species Enterococcus faecalis [TaxId:1351] [419402] (8 PDB entries)

8. Domain d1nhsa1: 1nhs A:1-119,A:243-321 [30555]
   Other proteins in same PDB: d1nhsa2, d1nhsa3
   complexed with fad, so4; mutant
   has additional insertions and/or extensions that are not grouped together

Details for d1nhsa1

PDB Entry: 1nhs, 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:

>d1nhsa1 c.3.1.5 (A:1-119,A:243-321) NADH peroxidase, N- and C-terminal domain {Enterococcus faecalis [TaxId: 1351]}
mkvivlgsshggyeaveellnlhpdaeiqwyekgdfisflccgmqlylegkvkdvnsvry
mtgekmesrgvnvfsnteitaiqpkehqvtvkdlvsgeervenydkliispgavpfeldX
gvrpntawlkgtlelhpngliktdeymrtsepdvfavgdatlikynpadtevnialatna
rkqgrfavknleepvkpfp

Timeline for d1nhsa1:

• d1nhsa1 first appeared (with stable ids) in SCOP 1.55, called d1nhs_1
  
• d1nhsa1 appears in SCOPe 2.07