SCOPe 2.08: Domain d1pdya1: 1pdy A:140-433

Lineage for d1pdya1 (1pdy A:140-433)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (34 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] (3 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] (2 proteins)
   automatically mapped to Pfam PF00113

6. Protein Enolase [51606] (11 species)
   Fold of this protein slightly differs from common fold in topology

7. Species European lobster (Homarus vulgaris) [TaxId:6707] [51608] (2 PDB entries)

8. Domain d1pdya1: 1pdy A:140-433 [29216]
   Other proteins in same PDB: d1pdya2
   complexed with so4

Details for d1pdya1

PDB Entry: 1pdy, 2.4 Å

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

PDB Compounds: (A:) enolase

SCOPe Domain Sequences for d1pdya1:

Sequence; same for both SEQRES and ATOM records:

>d1pdya1 c.1.11.1 (A:140-433) Enolase {European lobster (Homarus vulgaris) [TaxId: 6707]}
devilpvpafnvinggshagnklamqefmilptgatsfteamrmgtevyhhlkavikarf
gldatavgdeggfapnilnnkdaldliqeaikkagytgkieigmdvaasefykqnniydl
dfktanndgsqkisgdqlrdmymefckdfpivsiedpfdqddwetwskmtsgttiqivgd
dltvtnpkrittavekkackclllkvnqigsvtesidahllakkngwgtmvshrsgeted
cfiadlvvglctgqiktgapcrserlakynqilrieeelgsgakfagknfraps

Timeline for d1pdya1:

• d1pdya1 first appeared (with stable ids) in SCOP 1.55, called d1pdy_1
  
• d1pdya1 appears in SCOPe 2.07