SCOPe 2.05: Domain d1i5za2: 1i5z A:6-137

Lineage for d1i5za2 (1i5z A:6-137)

1. Root: SCOPe 2.05

2. Class b: All beta proteins [48724] (176 folds)

3. Fold b.82: Double-stranded beta-helix [51181] (7 superfamilies)
   one turn of helix is made by two pairs of antiparallel strands linked with short turns
   has appearance of a sandwich of distinct architecture and jelly-roll topology

4. Superfamily b.82.3: cAMP-binding domain-like [51206] (4 families)

5. Family b.82.3.2: cAMP-binding domain [51210] (13 proteins)
   Pfam PF00027

6. Protein Catabolite gene activator protein, N-terminal domain [51211] (1 species)

7. Species Escherichia coli [TaxId:562] [51212] (30 PDB entries)

8. Domain d1i5za2: 1i5z A:6-137 [83670]
   Other proteins in same PDB: d1i5za1, d1i5zb1
   complexed with cmp, trs

Details for d1i5za2

PDB Entry: 1i5z, 1.9 Å

PDB Description: structure of crp-camp at 1.9 a

PDB Compounds: (A:) catabolite gene activator protein

SCOPe Domain Sequences for d1i5za2:

Sequence; same for both SEQRES and ATOM records:

>d1i5za2 b.82.3.2 (A:6-137) Catabolite gene activator protein, N-terminal domain {Escherichia coli [TaxId: 562]}
qtdptlewflshchihkypskstlihqgekaetlyyivkgsvavlikdeegkemilsyln
qgdfigelglfeegqersawvraktacevaeisykkfrqliqvnpdilmrlsaqmarrlq
vtsekvgnlafl

Timeline for d1i5za2:

• d1i5za2 first appeared in SCOP 1.65
  
• d1i5za2 appears in SCOPe 2.04
  
• d1i5za2 appears in SCOPe 2.06
  
• d1i5za2 appears in the current release, SCOPe 2.08