Lineage for d1piia1 (1pii A:255-452)

  1. Root: SCOPe 2.07
  2. 2434694Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2434695Fold 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. 2435328Superfamily c.1.2: Ribulose-phoshate binding barrel [51366] (7 families) (S)
  5. 2435860Family c.1.2.4: Tryptophan biosynthesis enzymes [51381] (4 proteins)
  6. 2435879Protein N-(5'phosphoribosyl)antranilate isomerase, PRAI [51382] (3 species)
  7. 2435880Species Escherichia coli [TaxId:562] [51383] (1 PDB entry)
    merged in bifunctional enzyme with IPG synthase
  8. 2435881Domain d1piia1: 1pii A:255-452 [28559]
    Other proteins in same PDB: d1piia2
    complexed with po4

Details for d1piia1

PDB Entry: 1pii (more details), 2 Å

PDB Description: three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from escherichia coli refined at 2.0 angstroms resolution
PDB Compounds: (A:) n-(5'phosphoribosyl)anthranilate isomerase

SCOPe Domain Sequences for d1piia1:

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

>d1piia1 c.1.2.4 (A:255-452) N-(5'phosphoribosyl)antranilate isomerase, PRAI {Escherichia coli [TaxId: 562]}

SCOPe Domain Coordinates for d1piia1:

Click to download the PDB-style file with coordinates for d1piia1.
(The format of our PDB-style files is described here.)

Timeline for d1piia1:

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