SCOP 1.73: Domain d5enla1: 5enl A:142-436

Lineage for d5enla1 (5enl A:142-436)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 folds)

3. Fold c.1: TIM beta/alpha-barrel [51350] (33 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 superfamily

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

6. Protein Enolase [51606] (7 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 d5enla1: 5enl A:142-436 [29207]
   Other proteins in same PDB: d5enla2
   complexed with 2pg, ca

Details for d5enla1

PDB Entry: 5enl, 2.2 Å

PDB Description: inhibition of enolase: the crystal structures of enolase-ca2+- phosphoglycerate and enolase-zn2+-phosphoglycolate complexes at 2.2- angstroms resolution

PDB Compounds: (A:) enolase

SCOP Domain Sequences for d5enla1:

Sequence; same for both SEQRES and ATOM records:

>d5enla1 c.1.11.1 (A:142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl

Timeline for d5enla1:

• d5enla1 first appeared (with stable ids) in SCOP 1.55, called d5enl_1
  
• d5enla1 was called d5enl_1 in SCOP 1.71
  
• d5enla1 appears in SCOP 1.75
  
• d5enla1 appears in the current release, SCOPe 2.08