SCOP 1.67: Domain d1nel_1: 1nel 142-436

Lineage for d1nel_1 (1nel 142-436)

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 d1nel_1: 1nel 142-436 [29214]
   Other proteins in same PDB: d1nel_2
   complexed with f f, mg, po4

Details for d1nel_1

PDB Entry: 1nel, 2.6 Å

PDB Description: fluoride inhibition of yeast enolase: crystal structure of the enolase-mg2+-f--pi complex at 2.6-angstroms resolution

SCOP Domain Sequences for d1nel_1:

Sequence; same for both SEQRES and ATOM records:

>d1nel_1 c.1.11.1 (142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae)}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl

Timeline for d1nel_1:

• d1nel_1 first appeared (with stable ids) in SCOP 1.55
  
• d1nel_1 appears in SCOP 1.65
  
• d1nel_1 appears in SCOP 1.69
  
• d1nel_1 appears in the current release, SCOPe 2.08, called d1nela1