SCOPe 2.06: Domain d1o5kb1: 1o5k B:1-294

Lineage for d1o5kb1 (1o5k B:1-294)

1. Root: SCOPe 2.06

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

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 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] (9 families)
   Common fold covers whole protein structure

5. Family c.1.10.1: Class I aldolase [51570] (13 proteins)
   the catalytic lysine forms schiff-base intermediate with substrate
   possible link between the aldolase superfamily and the phosphate-binding beta/alpha barrels

6. Protein Dihydrodipicolinate synthase [51574] (13 species)

7. Species Thermotoga maritima [TaxId:2336] [102090] (1 PDB entry)

8. Domain d1o5kb1: 1o5k B:1-294 [92505]
   Other proteins in same PDB: d1o5ka2, d1o5kb2
   structural genomics
   complexed with ca

Details for d1o5kb1

PDB Entry: 1o5k, 1.8 Å

PDB Description: crystal structure of dihydrodipicolinate synthase (tm1521) from thermotoga maritima at 1.80 a resolution

PDB Compounds: (B:) Dihydrodipicolinate synthase

SCOPe Domain Sequences for d1o5kb1:

Sequence; same for both SEQRES and ATOM records:

>d1o5kb1 c.1.10.1 (B:1-294) Dihydrodipicolinate synthase {Thermotoga maritima [TaxId: 2336]}
mfrgvgtaivtpfkngeldlesyerlvryqlengvnalivlgttgesptvnedereklvs
rtleivdgkipvivgagtnstektlklvkqaeklgangvlvvtpyynkptqeglyqhyky
isertdlgivvynvpgrtgvnvlpetaariaadlknvvgikeanpdidqidrtvsltkqa
rsdfmvwsgnddrtfyllcaggdgvisvvsnvapkqmvelcaeyfsgnleksrevhrklr
plmkalfvetnpipvkaalnlmgfienelrlplvpasektvellrnvlkesgll

Timeline for d1o5kb1:

• d1o5kb1 first appeared in SCOP 1.67, called d1o5kb_
  
• d1o5kb1 was called d1o5kb_ in SCOPe 2.05
  
• d1o5kb1 appears in SCOPe 2.07
  
• d1o5kb1 appears in the current release, SCOPe 2.08