SCOPe 2.08: Domain d1elsa1: 1els A:142-436

Lineage for d1elsa1 (1els A:142-436)

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 d1elsa1: 1els A:142-436 [29213]
   Other proteins in same PDB: d1elsa2
   complexed with mn, pah

Details for d1elsa1

PDB Entry: 1els, 2.4 Å

PDB Description: catalytic metal ion binding in enolase: the crystal structure of enolase-mn2+-phosphonoacetohydroxamate complex at 2.4 angstroms resolution

PDB Compounds: (A:) enolase

SCOPe Domain Sequences for d1elsa1:

Sequence; same for both SEQRES and ATOM records:

>d1elsa1 c.1.11.1 (A:142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl

Timeline for d1elsa1:

• d1elsa1 first appeared (with stable ids) in SCOP 1.55, called d1els_1
  
• d1elsa1 appears in SCOPe 2.07