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Lineage for d1piia2 (1pii A:1-254)

  1. Root: SCOPe 2.06
  2. 2078559Class c: Alpha and beta proteins (a/b) [51349] (148 folds)
  3. 2078560Fold 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. 2079053Superfamily c.1.2: Ribulose-phoshate binding barrel [51366] (7 families) (S)
  5. 2079565Family c.1.2.4: Tryptophan biosynthesis enzymes [51381] (4 protein domains)
  6. 2079566Protein Indole-3-glycerophosphate synthase, IPGS [51385] (4 species)
  7. 2079567Species Escherichia coli [TaxId:562] [51386] (2 PDB entries)
    merged in bifunctional enzyme with PRA isomerase
  8. 2079568Domain d1piia2: 1pii A:1-254 [28563]
    Other proteins in same PDB: d1piia1
    complexed with po4

Details for d1piia2

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 d1piia2:

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

>d1piia2 c.1.2.4 (A:1-254) Indole-3-glycerophosphate synthase, IPGS {Escherichia coli [TaxId: 562]}
mqtvlakivadkaiwvearkqqqplasfqnevqpstrhfydalqgartafileckkasps
kgvirddfdpariaaiykhyasaisvltdekyfqgsfnflpivsqiapqpilckdfiidp
yqiylaryyqadacllmlsvldddqyrqlaavahslemgvltevsneeeqeraialgakv
vginnrdlrdlsidlnrtrelapklghnvtvisesgintyaqvrelshfangfligsalm
ahddlhaavrrvll

SCOPe Domain Coordinates for d1piia2:

Click to download the PDB-style file with coordinates for d1piia2.
(The format of our PDB-style files is described here.)

Timeline for d1piia2:

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Domains from same chain:
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d1piia1