SCOPe 2.08: Domain d1p43b1: 1p43 B:642-936

Lineage for d1p43b1 (1p43 B:642-936)

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 Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [51607] (16 PDB entries)

8. Domain d1p43b1: 1p43 B:642-936 [94074]
   Other proteins in same PDB: d1p43a2, d1p43b2
   complexed with 2pg, mg

Details for d1p43b1

PDB Entry: 1p43, 1.8 Å

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

PDB Compounds: (B:) enolase 1

SCOPe Domain Sequences for d1p43b1:

Sequence; same for both SEQRES and ATOM records:

>d1p43b1 c.1.11.1 (B:642-936) Enolase {Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]}
spyvlpvpflnvlnggshaggalalqqfmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl

Timeline for d1p43b1:

• d1p43b1 first appeared in SCOP 1.67
  
• d1p43b1 appears in SCOPe 2.07