SCOPe 2.06: Domain d5t26b1: 5t26 B:1-292

Lineage for d5t26b1 (5t26 B:1-292)

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 Escherichia coli [TaxId:585034] [323806] (2 PDB entries)

8. Domain d5t26b1: 5t26 B:1-292 [323807]
   Other proteins in same PDB: d5t26a2, d5t26b2
   automated match to d2atsa_
   complexed with gol, na, tla

Details for d5t26b1

PDB Entry: 5t26, 2.1 Å

PDB Description: kinetic, spectral and structural characterization of the slow binding inhibitor acetopyruvate with dihydrodipicolinate synthase from escherichia coli.

PDB Compounds: (B:) 4-hydroxy-tetrahydrodipicolinate synthase

SCOPe Domain Sequences for d5t26b1:

Sequence; same for both SEQRES and ATOM records:

>d5t26b1 c.1.10.1 (B:1-292) Dihydrodipicolinate synthase {Escherichia coli [TaxId: 585034]}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigixeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll

Timeline for d5t26b1:

• d5t26b1 is new in SCOPe 2.06-stable
  
• d5t26b1 appears in SCOPe 2.07
  
• d5t26b1 appears in the current release, SCOPe 2.08