Lineage for d1ecjd2 (1ecj D:1-249)

  1. Root: SCOPe 2.08
  2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)
  3. Fold d.153: Ntn hydrolase-like [56234] (2 superfamilies)
    4 layers: alpha/beta/beta/alpha; has an unusual sheet-to-sheet packing
  4. Superfamily d.153.1: N-terminal nucleophile aminohydrolases (Ntn hydrolases) [56235] (8 families) (S)
    N-terminal residue provides two catalytic groups, nucleophile and proton donor
  5. Family d.153.1.1: Class II glutamine amidotransferases [56236] (6 proteins)
    has slightly different topology than other families do
  6. Protein Glutamine PRPP amidotransferase, N-terminal domain [56239] (3 species)
  7. Species Escherichia coli [TaxId:562] [56241] (5 PDB entries)
  8. Domain d1ecjd2: 1ecj D:1-249 [41829]
    Other proteins in same PDB: d1ecja1, d1ecjb1, d1ecjc1, d1ecjd1
    complexed with amp

Details for d1ecjd2

PDB Entry: 1ecj (more details), 2.5 Å

PDB Description: escherichia coli glutamine phosphoribosylpyrophosphate (prpp) amidotransferase complexed with 2 amp per tetramer
PDB Compounds: (D:) glutamine phosphoribosylpyrophosphate amidotransferase

SCOPe Domain Sequences for d1ecjd2:

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

>d1ecjd2 d.153.1.1 (D:1-249) Glutamine PRPP amidotransferase, N-terminal domain {Escherichia coli [TaxId: 562]}
cgivgiagvmpvnqsiydaltvlqhrgqdaagiitidanncfrlrkanglvsdvfearhm
qrlqgnmgighvryptagsssaseaqpfyvnspygitlahngnltnahelrkklfeekrr
hinttsdseillnifaseldnfrhypleadnifaaiaatnrlirgayacvamiighgmva
frdpngirplvlgkrdidenrteymvasesvaldtlgfdflrdvapgeaiyiteegqlft
rqcadnpvs

SCOPe Domain Coordinates for d1ecjd2 are not available.

Timeline for d1ecjd2:

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Domains from same chain:
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d1ecjd1
View in 3D
Domains from other chains:
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d1ecja1, d1ecja2, d1ecjb1, d1ecjb2, d1ecjc1, d1ecjc2