SCOP 1.71: Domain d1pdz_1: 1pdz 140-433

Lineage for d1pdz_1 (1pdz 140-433)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (32 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.1.11: Enolase C-terminal domain-like [51604] (2 families)
   binds metal ion (magnesium or manganese) in conserved site inside barrel
   N-terminal alpha+beta domain is common to this superfamily

5. Family c.1.11.1: Enolase [51605] (1 protein)

6. Protein Enolase [51606] (6 species)
   Fold of this protein slightly differs from common fold in topology

7. Species Lobster (Homarus vulgaris) [51608] (2 PDB entries)

8. Domain d1pdz_1: 1pdz 140-433 [29215]
   Other proteins in same PDB: d1pdz_2
   complexed with mn, pga

Details for d1pdz_1

PDB Entry: 1pdz, 2.2 Å

PDB Description: x-ray structure and catalytic mechanism of lobster enolase

SCOP Domain Sequences for d1pdz_1:

Sequence; same for both SEQRES and ATOM records:

>d1pdz_1 c.1.11.1 (140-433) Enolase {Lobster (Homarus vulgaris)}
devilpvpafnvinggshagnklamqefmilptgatsfteamrmgtevyhhlkavikarf
gldatavgdeggfapnilnnkdaldliqeaikkagytgkieigmdvaasefykqnniydl
dfktanndgsqkisgdqlrdmymefckdfpivsiedpfdqddwetwskmtsgttiqivgd
dltvtnpkrittavekkackclllkvnqigsvtesidahllakkngwgtmvshrsgeted
cfiadlvvglctgqiktgapcrserlakynqilrieeelgsgakfagknfraps

Timeline for d1pdz_1:

• d1pdz_1 first appeared (with stable ids) in SCOP 1.55
  
• d1pdz_1 appears in SCOP 1.69
  
• d1pdz_1 is called d1pdza1 in SCOP 1.73
  
• d1pdz_1 appears in the current release, SCOPe 2.08, called d1pdza1