SCOPe 2.06: Domain d5idza2: 5idz A:141-434

Lineage for d5idza2 (5idz A:141-434)

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 Human (Homo sapiens), gamma isoform [TaxId:9606] [110371] (15 PDB entries)
   Uniprot P09104

8. Domain d5idza2: 5idz A:141-434 [330023]
   Other proteins in same PDB: d5idza1, d5idza3, d5idzb1
   automated match to d2akza1
   complexed with 6bm, mg, pge

Details for d5idza2

PDB Entry: 5idz, 2.63 Å

PDB Description: structure of human enolase 2 in complex with (s)-(1-hydroxy-2- oxopiperidin-3-yl)phosphonate

PDB Compounds: (A:) Gamma-enolase

SCOPe Domain Sequences for d5idza2:

Sequence; same for both SEQRES and ATOM records:

>d5idza2 c.1.11.1 (A:141-434) Enolase {Human (Homo sapiens), gamma isoform [TaxId: 9606]}
sdlilpvpafnvinggshagnklamqefmilpvgaesfrdamrlgaevyhtlkgvikdky
gkdatnvgdeggfapnilensealelvkeaidkagytekivigmdvaasefyrdgkydld
fksptdpsryitgdqlgalyqdfvrdypvvsiedpfdqddwaawskftanvgiqivgddl
tvtnpkrieraveekacnclllkvnqigsvteaiqacklaqengwgvmvshrsgetedtf
iadlvvglctgqiktgapcrserlakynqlmrieeelgdearfaghnfrnpsvl

Timeline for d5idza2:

• d5idza2 is new in SCOPe 2.06-stable
  
• d5idza2 appears in SCOPe 2.07
  
• d5idza2 appears in the current release, SCOPe 2.08