SCOP 1.67: Domain d1p48b1: 1p48 B:642-936

Lineage for d1p48b1 (1p48 B:642-936)

1. Root: SCOP 1.67

2. Class c: Alpha and beta proteins (a/b) [51349] (130 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (28 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 family

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

6. Protein Enolase [51606] (5 species)
   Fold of this protein slightly differs from common fold in topology

7. Species Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [51607] (14 PDB entries)

8. Domain d1p48b1: 1p48 B:642-936 [94087]
   Other proteins in same PDB: d1p48a2, d1p48b2
   complexed with mg, pep; mutant

Details for d1p48b1

PDB Entry: 1p48, 2 Å

PDB Description: reverse protonation is the key to general acid-base catalysis in enolase

SCOP Domain Sequences for d1p48b1:

Sequence; same for both SEQRES and ATOM records:

>d1p48b1 c.1.11.1 (B:642-936) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdqggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl

Timeline for d1p48b1:

• d1p48b1 is new in SCOP 1.67
  
• d1p48b1 appears in SCOP 1.69
  
• d1p48b1 appears in the current release, SCOPe 2.08