SCOP 1.69: Domain d1fwrb_: 1fwr B:

Lineage for d1fwrb_ (1fwr B:)

1. Root: SCOP 1.69

2. Class c: Alpha and beta proteins (a/b) [51349] (136 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (31 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] (6 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 KDPG aldolase [51584] (3 species)

7. Species Escherichia coli [TaxId:562] [51585] (4 PDB entries)

8. Domain d1fwrb_: 1fwr B: [29165]

Details for d1fwrb_

PDB Entry: 1fwr, 2.7 Å

PDB Description: crystal structure of kdpg aldolase double mutant k133q/t161k

SCOP Domain Sequences for d1fwrb_:

Sequence; same for both SEQRES and ATOM records:

>d1fwrb_ c.1.10.1 (B:) KDPG aldolase {Escherichia coli}
mknwktsaesilttgpvvpvivvkklehavpmakalvaggvrvlevtlrtecavdairai
akevpeaivgagtvlnpqqlaevteagaqfaispgltepllkaategtiplipgistvse
lmlgmdyglkefqffpaeanggvkalqaiagpfsqvrfcpkggispanyrdylalksvlc
iggswlvpadaleagdydritklareavegakl

Timeline for d1fwrb_:

• d1fwrb_ first appeared (with stable ids) in SCOP 1.55
  
• d1fwrb_ appears in SCOP 1.67
  
• d1fwrb_ appears in SCOP 1.71
  
• d1fwrb_ appears in the current release, SCOPe 2.08