Lineage for d1pdy_1 (1pdy 140-433)

  1. Root: SCOP 1.67
  2. 383641Class c: Alpha and beta proteins (a/b) [51349] (130 folds)
  3. 383642Fold c.1: TIM beta/alpha-barrel [51350] (28 superfamilies)
    contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
    the first seven superfamilies have similar phosphate-binding sites
  4. 386021Superfamily c.1.11: Enolase C-terminal domain-like [51604] (2 families) (S)
    binds metal ion (magnesium or manganese) in conserved site inside barrel
    N-terminal alpha+beta domain is common to this family
  5. 386022Family c.1.11.1: Enolase [51605] (1 protein)
  6. 386023Protein Enolase [51606] (5 species)
    Fold of this protein slightly differs from common fold in topology
  7. 386056Species Lobster (Homarus vulgaris) [51608] (2 PDB entries)
  8. 386058Domain d1pdy_1: 1pdy 140-433 [29216]
    Other proteins in same PDB: d1pdy_2
    complexed with so4

Details for d1pdy_1

PDB Entry: 1pdy (more details), 2.4 Å

PDB Description: x-ray structure and catalytic mechanism of lobster enolase
PDB Compounds: ( :)

SCOP Domain Sequences for d1pdy_1:

Sequence; same for both SEQRES and ATOM records: (download)

>d1pdy_1 c.1.11.1 (140-433) Enolase {Lobster (Homarus vulgaris)}

SCOP Domain Coordinates for d1pdy_1:

Click to download the PDB-style file with coordinates for d1pdy_1.
(The format of our PDB-style files is described here.)

Timeline for d1pdy_1:

View in 3D
Domains from same chain:
(mouse over for more information)