SCOPe 2.04: Domain d2a6na1: 2a6n A:1-292

Lineage for d2a6na1 (2a6n A:1-292)

1. Root: SCOPe 2.04

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] (12 species)

7. Species Escherichia coli [TaxId:562] [51575] (15 PDB entries)

8. Domain d2a6na1: 2a6n A:1-292 [126289]
   complexed with k; mutant

Details for d2a6na1

PDB Entry: 2a6n, 1.94 Å

PDB Description: dihydrodipicolinate synthase (e. coli)- mutant r138a

PDB Compounds: (A:) Dihydrodipicolinate synthase

SCOPe Domain Sequences for d2a6na1:

Sequence; same for both SEQRES and ATOM records:

>d2a6na1 c.1.10.1 (A:1-292) Dihydrodipicolinate synthase {Escherichia coli [TaxId: 562]}
mftgsivaivtpmdekgnvcraslkklidyhvasgtsaivsvgttgesatlnhdehadvv
mmtldladgripviagtganataeaisltqrfndsgivgcltvtpyynrpsqeglyqhfk
aiaehtdlpqilynvpsatgcdllpetvgrlakvkniigikeatgnltrvnqikelvsdd
fvllsgddasaldfmqlgghgvisvtanvaardmaqmcklaaeghfaearvinqrlmplh
nklfvepnpipvkwackelglvatdtlrlpmtpitdsgretvraalkhagll

Timeline for d2a6na1:

• d2a6na1 first appeared in SCOP 1.73
  
• d2a6na1 appears in SCOPe 2.03
  
• d2a6na1 appears in SCOPe 2.05
  
• d2a6na1 appears in the current release, SCOPe 2.08