SCOP 1.71: Protein: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain

Lineage for Protein: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain

Root: SCOP 1.71
Class d: Alpha and beta proteins (a+b) [53931] (286 folds)
Fold d.58: Ferredoxin-like [54861] (51 superfamilies)
alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2
Superfamily d.58.18: ACT-like [55021] (5 families)
regulatory domain linked to a wide range of metabolic enzymes
Family d.58.18.1: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain [55022] (1 protein)
Protein Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain [55023] (1 species)

Species:

Escherichia coli [TaxId:562] [55024] (1 PDB entry)
- Domains for 1psd:
  1. Domain d1psda3: 1psd A:327-410 [39354]
    Other proteins in same PDB: d1psda1, d1psda2, d1psdb1, d1psdb2
  2. Domain d1psdb3: 1psd B:327-410 [39355]
    Other proteins in same PDB: d1psda1, d1psda2, d1psdb1, d1psdb2
    complexed with nad

More info for Protein Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain from d.58.18.1: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain

Timeline for Protein Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain from d.58.18.1: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain:

Protein Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain from d.58.18.1: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain first appeared (with stable ids) in SCOP 1.55
Protein Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain from d.58.18.1: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain appears in SCOP 1.69
Protein Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain from d.58.18.1: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain appears in SCOP 1.73
Protein Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain from d.58.18.1: Phosphoglycerate dehydrogenase, regulatory (C-terminal) domain appears in the current release, SCOPe 2.08