SCOPe 2.03: Domain d2ptxa1: 2ptx A:139-429

Lineage for d2ptxa1 (2ptx A:139-429)

1. Root: SCOPe 2.03

2. Class c: Alpha and beta proteins (a/b) [51349] (147 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] (9 species)
   Fold of this protein slightly differs from common fold in topology

7. Species Trypanosome (Trypanosoma brucei) [TaxId:5691] [159415] (6 PDB entries)

8. Domain d2ptxa1: 2ptx A:139-429 [149840]
   Other proteins in same PDB: d2ptxa2
   automatically matched to d1oepa1
   complexed with edo, so4, zn

Details for d2ptxa1

PDB Entry: 2ptx, 1.9 Å

PDB Description: crystal structure of the t. brucei enolase complexed with sulphate in closed conformation

PDB Compounds: (A:) enolase

SCOPe Domain Sequences for d2ptxa1:

Sequence; same for both SEQRES and ATOM records:

>d2ptxa1 c.1.11.1 (A:139-429) Enolase {Trypanosome (Trypanosoma brucei) [TaxId: 5691]}
kelrlpvpcfnvinggkhagnalpfqefmiapvkatsfsealrmgsevyhslrgiikkky
gqdavnvgdeggfappikdineplpilmeaieeaghrgkfaicmdcaasetydekkqqyn
ltfkspeptwvtaeqlretyckwahdypivsiedpydqddfagfagitealkgktqivgd
dltvtnterikmaiekkacnslllkinqigtiseaiassklcmengwsvmvshrsgeted
tyiadlvvalgsgqiktgapcrgertaklnqllrieeelgahakfgfpgws

Timeline for d2ptxa1:

• d2ptxa1 first appeared in SCOP 1.75
  
• d2ptxa1 appears in SCOPe 2.02
  
• d2ptxa1 appears in SCOPe 2.04
  
• d2ptxa1 appears in the current release, SCOPe 2.08