SCOP 1.73: Domain d2akmb1: 2akm B:140-432

Lineage for d2akmb1 (2akm B:140-432)

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 Human (Homo sapiens), gamma isoform [TaxId:9606] [110371] (3 PDB entries)

8. Domain d2akmb1: 2akm B:140-432 [126921]
   Other proteins in same PDB: d2akma2, d2akmb2
   automatically matched to d1te6a1
   complexed with mg, po4, trs

Details for d2akmb1

PDB Entry: 2akm, 1.92 Å

PDB Description: Fluoride Inhibition of Enolase: Crystal Structure of the Inhibitory Complex

PDB Compounds: (B:) Gamma enolase

SCOP Domain Sequences for d2akmb1:

Sequence; same for both SEQRES and ATOM records:

>d2akmb1 c.1.11.1 (B:140-432) Enolase {Human (Homo sapiens), gamma isoform [TaxId: 9606]}
sdlilpvpafnvinggshagnklamqefmilpvgaesfrdamrlgaevyhtlkgvikdky
gkdatnvgdeggfapnilensealelvkeaidkagytekivigmdvaasefyrdgkydld
fksptdpsryitgdqlgalyqdfvrdypvvsiedpfdqddwaawskftanvgiqivgddl
tvtnpkrieraveekacnclllkvnqigsvteaiqacklaqengwgvmvshrsgetedtf
iadlvvglctgqiktgapcrserlakynqlmrieeelgdearfaghnfrnpsv

Timeline for d2akmb1:

• d2akmb1 is new in SCOP 1.73
  
• d2akmb1 appears in SCOP 1.75
  
• d2akmb1 appears in the current release, SCOPe 2.08