SCOPe 2.06: Domain d3i7sa_: 3i7s A:

Lineage for d3i7sa_ (3i7s A:)

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 K-12 [TaxId:83333] [188673] (3 PDB entries)

8. Domain d3i7sa_: 3i7s A: [178137]
   automated match to d1dhpa_
   complexed with gol, k, po4, pyr; mutant

Details for d3i7sa_

PDB Entry: 3i7s, 2.3 Å

PDB Description: dihydrodipicolinate synthase mutant - k161a - with the substrate pyruvate bound in the active site.

PDB Compounds: (A:) Dihydrodipicolinate synthase

SCOPe Domain Sequences for d3i7sa_:

Sequence; same for both SEQRES and ATOM records:

>d3i7sa_ c.1.10.1 (A:) Dihydrodipicolinate synthase {Escherichia coli K-12 [TaxId: 83333]}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigireatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll

Timeline for d3i7sa_:

• d3i7sa_ first appeared in SCOPe 2.01
  
• d3i7sa_ appears in SCOPe 2.05
  
• d3i7sa_ appears in SCOPe 2.07
  
• d3i7sa_ appears in the current release, SCOPe 2.08