Lineage for d5t25b_ (5t25 B:)

  1. Root: SCOPe 2.06
  2. 2089713Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2089714Fold 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. 2096922Superfamily c.1.10: Aldolase [51569] (9 families) (S)
    Common fold covers whole protein structure
  5. 2096923Family 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. 2097054Protein Dihydrodipicolinate synthase [51574] (13 species)
  7. 2097126Species Escherichia coli [TaxId:585034] [323806] (2 PDB entries)
  8. 2097128Domain d5t25b_: 5t25 B: [330478]
    Other proteins in same PDB: d5t25a2
    automated match to d3du0a_
    complexed with lys, na

Details for d5t25b_

PDB Entry: 5t25 (more details), 1.99 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 d5t25b_:

Sequence; same for both SEQRES and ATOM records: (download)

>d5t25b_ c.1.10.1 (B:) Dihydrodipicolinate synthase {Escherichia coli [TaxId: 585034]}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigixeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll

SCOPe Domain Coordinates for d5t25b_:

Click to download the PDB-style file with coordinates for d5t25b_.
(The format of our PDB-style files is described here.)

Timeline for d5t25b_: