SCOP 1.73: Domain d1yxda1: 1yxd A:1-292

Lineage for d1yxda1 (1yxd A:1-292)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 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] (8 families)
   Common fold covers whole protein structure

5. Family c.1.10.1: Class I aldolase [51570] (12 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] (4 species)

7. Species Escherichia coli [TaxId:562] [51575] (9 PDB entries)

8. Domain d1yxda1: 1yxd A:1-292 [124185]
   automatically matched to d1dhpa_
   complexed with cl, k, lys

Details for d1yxda1

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

SCOP Domain Sequences for d1yxda1:

Sequence; same for both SEQRES and ATOM records:

>d1yxda1 c.1.10.1 (A:1-292) Dihydrodipicolinate synthase {Escherichia coli [TaxId: 562]}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsrtgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll

Timeline for d1yxda1:

• d1yxda1 is new in SCOP 1.73
  
• d1yxda1 appears in SCOP 1.75
  
• d1yxda1 appears in the current release, SCOPe 2.08, called d1yxda_