SCOPe 2.07: Domain d1yxda_: 1yxd A:

Lineage for d1yxda_ (1yxd A:)

1. Root: SCOPe 2.07

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:562] [51575] (17 PDB entries)

8. Domain d1yxda_: 1yxd A: [124185]
   automated match to d1dhpa_
   complexed with cl, k, lys

Details for d1yxda_

PDB Entry: 1yxd, 2 Å

PDB Description: structure of e. coli dihydrodipicolinate synthase bound with allosteric inhibitor (s)-lysine to 2.0 a

PDB Compounds: (A:) Dihydrodipicolinate synthase

SCOPe Domain Sequences for d1yxda_:

Sequence; same for both SEQRES and ATOM records:

>d1yxda_ c.1.10.1 (A:) Dihydrodipicolinate synthase {Escherichia coli [TaxId: 562]}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll

Timeline for d1yxda_:

• d1yxda_ first appeared in SCOP 1.73, called d1yxda1
  
• d1yxda_ appears in SCOPe 2.06
  
• d1yxda_ appears in the current release, SCOPe 2.08