SCOP 1.65: Domain d1nvma2: 1nvm A:2-290

Lineage for d1nvma2 (1nvm A:2-290)

1. Root: SCOP 1.65

2. Class c: Alpha and beta proteins (a/b) [51349] (121 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (26 superfamilies)
   contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
   the first seven superfamilies have similar phosphate-binding sites

4. Superfamily c.1.10: Aldolase [51569] (5 families)
   Common fold covers whole protein structure

5. Family c.1.10.5: 4-hydroxy-2-oxovalerate aldolase DmpG, catalytic domain [89494] (1 protein)

6. Protein 4-hydroxy-2-oxovalerate aldolase DmpG, catalytic domain [89495] (1 species)

7. Species Pseudomonas sp. [TaxId:306] [89496] (1 PDB entry)
   gene product DmpG

8. Domain d1nvma2: 1nvm A:2-290 [86250]
   Other proteins in same PDB: d1nvma1, d1nvmb1, d1nvmb2, d1nvmc1, d1nvmd1, d1nvmd2, d1nvme1, d1nvmf1, d1nvmf2, d1nvmg1, d1nvmh1, d1nvmh2

Details for d1nvma2

PDB Entry: 1nvm, 1.7 Å

PDB Description: crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate

SCOP Domain Sequences for d1nvma2:

Sequence; same for both SEQRES and ATOM records:

>d1nvma2 c.1.10.5 (A:2-290) 4-hydroxy-2-oxovalerate aldolase DmpG, catalytic domain {Pseudomonas sp.}
tfnpskklyisdvtlrdgshairhqytlddvraiaraldkakvdsievahgdglqgssfn
ygfgrhtdleyieavageishaqiatlllpgigsvhdlknayqagarvvrvathcteadv
skqhieyarnlgmdtvgflmmshmipaeklaeqgklmesygatciymadsggamsmndir
drmrafkavlkpetqvgmhahhnlslgvansivaveegcdrvdaslagmgagagnaplev
fiavaerlgwnhgtdlytlmdaaddivrplqdrpvrvdretlglgyagv

Timeline for d1nvma2:

• d1nvma2 is new in SCOP 1.65
  
• d1nvma2 appears in SCOP 1.67
  
• d1nvma2 appears in the current release, SCOPe 2.08