SCOPe 2.06: Domain d5dx6a3: 5dx6 A:367-554

Lineage for d5dx6a3 (5dx6 A:367-554)

1. Root: SCOPe 2.06

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

3. Fold c.36: Thiamin diphosphate-binding fold (THDP-binding) [52517] (1 superfamily)
   3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465

4. Superfamily c.36.1: Thiamin diphosphate-binding fold (THDP-binding) [52518] (9 families)
   there are two different functional modules of this fold: pyridine-binding (Pyr) and pyrophosphate-binding (PP) modules
   two Pyr and two PP modules assemble together in a conserved heterotetrameric core that binds two THDP coenzyme molecules

5. Family c.36.1.0: automated matches [227300] (1 protein)
   not a true family

6. Protein automated matches [227126] (20 species)
   not a true protein

7. Species Klebsiella pneumoniae [TaxId:573] [319715] (2 PDB entries)

8. Domain d5dx6a3: 5dx6 A:367-554 [323339]
   Other proteins in same PDB: d5dx6a2, d5dx6b2, d5dx6b4
   automated match to d1ozga3
   complexed with 5gy, 65s, mg, po4, tpp

Details for d5dx6a3

PDB Entry: 5dx6, 1.75 Å

PDB Description: acetolactate synthase from klebsiella pneumoniae soaked with beta- fluoropyruvate

PDB Compounds: (A:) Acetolactate synthase, catabolic

SCOPe Domain Sequences for d5dx6a3:

Sequence; same for both SEQRES and ATOM records:

>d5dx6a3 c.36.1.0 (A:367-554) automated matches {Klebsiella pneumoniae [TaxId: 573]}
nqfalhplrivramqdivnsdvtltvdmgsfhiwiarylysfrarqvmisngqqtmgval
pwaigawlvnperkvvsvsgdggflqssmeletavrlkanvlhliwvdngynmvaiqeek
kyqrlsgvefgpmdfkayaesfgakgfavesaealeptlraamdvdgpavvaipvdyrdn
pllmgqlh

Timeline for d5dx6a3:

• d5dx6a3 is new in SCOPe 2.06-stable
  
• d5dx6a3 appears in SCOPe 2.07
  
• d5dx6a3 appears in the current release, SCOPe 2.08