SCOPe 2.06: Domain d4enla1: 4enl A:142-436

Lineage for d4enla1 (4enl A:142-436)

1. Root: SCOPe 2.06

2. Class c: Alpha and beta proteins (a/b) [51349] (148 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] (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] (10 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 d4enla1: 4enl A:142-436 [29202]
   Other proteins in same PDB: d4enla2
   complexed with so4, zn

Details for d4enla1

PDB Entry: 4enl, 1.9 Å

PDB Description: crystal structure of holoenzyme refined at 1.9 angstroms resolution: trigonal-bipyramidal geometry of the cation binding site

PDB Compounds: (A:) enolase

SCOPe Domain Sequences for d4enla1:

Sequence; same for both SEQRES and ATOM records:

>d4enla1 c.1.11.1 (A:142-436) Enolase {Baker's yeast (Saccharomyces cerevisiae) [TaxId: 4932]}
spyvlpvpflnvlnggshaggalalqefmiaptgaktfaealrigsevyhnlksltkkry
gasagnvgdeggvapniqtaeealdlivdaikaaghdgkvkigldcasseffkdgkydld
fknpnsdkskwltgpqladlyhslmkrypivsiedpfaeddweawshffktagiqivadd
ltvtnpkriataiekkaadalllkvnqigtlsesikaaqdsfaagwgvmvshrsgetedt
fiadlvvglrtgqiktgaparserlaklnqllrieeelgdnavfagenfhhgdkl

Timeline for d4enla1:

• d4enla1 first appeared (with stable ids) in SCOP 1.55, called d4enl_1
  
• d4enla1 appears in SCOPe 2.05
  
• d4enla1 appears in SCOPe 2.07
  
• d4enla1 appears in the current release, SCOPe 2.08