SCOPe 2.08: Domain d1vm6c3: 1vm6 C:1-96,C:183-214

Lineage for d1vm6c3 (1vm6 C:1-96,C:183-214)

1. Root: SCOPe 2.08

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

3. Fold c.2: NAD(P)-binding Rossmann-fold domains [51734] (1 superfamily)
   core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456
   The nucleotide-binding modes of this and the next two folds/superfamilies are similar

4. Superfamily c.2.1: NAD(P)-binding Rossmann-fold domains [51735] (13 families)

5. Family c.2.1.3: Glyceraldehyde-3-phosphate dehydrogenase-like, N-terminal domain [51800] (22 proteins)
   family members also share a common alpha+beta fold in C-terminal domain

6. Protein Dihydrodipicolinate reductase [51821] (3 species)

7. Species Thermotoga maritima [TaxId:2336] [110417] (1 PDB entry)
   Uniprot Q9X1K8

8. Domain d1vm6c3: 1vm6 C:1-96,C:183-214 [118632]
   Other proteins in same PDB: d1vm6a2, d1vm6a4, d1vm6b2, d1vm6b3, d1vm6c2, d1vm6d2, d1vm6d3
   Structural genomics target
   complexed with act, edo, nad, pg4

Details for d1vm6c3

PDB Entry: 1vm6, 2.27 Å

PDB Description: crystal structure of dihydrodipicolinate reductase (tm1520) from thermotoga maritima at 2.27 a resolution

PDB Compounds: (C:) dihydrodipicolinate reductase

SCOPe Domain Sequences for d1vm6c3:

Sequence; same for both SEQRES and ATOM records:

>d1vm6c3 c.2.1.3 (C:1-96,C:183-214) Dihydrodipicolinate reductase {Thermotoga maritima [TaxId: 2336]}
mkygivgysgrmgqeiqkvfsekghelvlkvdvngveeldspdvvidfsspealpktvdl
ckkyraglvlgttalkeehlqmlrelskevpvvqayXsrtvfaigalkaaeflvgkdpgm
ysfeevifg

Timeline for d1vm6c3:

• d1vm6c3 first appeared in SCOP 1.73
  
• d1vm6c3 appears in SCOPe 2.07