SCOPe 2.04: Domain d1raad2: 1raa D:101-153

Lineage for d1raad2 (1raa D:101-153)

1. Root: SCOPe 2.04

2. Class g: Small proteins [56992] (91 folds)

3. Fold g.41: Rubredoxin-like [57769] (17 superfamilies)
   metal(zinc or iron)-bound fold; sequence contains two CX(n)C motifs, in most cases n = 2

4. Superfamily g.41.7: Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain [57825] (2 families)
   automatically mapped to Pfam PF02748

5. Family g.41.7.1: Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain [57826] (1 protein)

6. Protein Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain [57827] (3 species)

7. Species Escherichia coli [TaxId:562] [57828] (60 PDB entries)
   Uniprot P00478

8. Domain d1raad2: 1raa D:101-153 [45286]
   Other proteins in same PDB: d1raaa1, d1raaa2, d1raab1, d1raac1, d1raac2, d1raad1
   complexed with ctp, zn; mutant

Details for d1raad2

PDB Entry: 1raa, 2.5 Å

PDB Description: crystal structure of ctp-ligated t state aspartate transcarbamoylase at 2.5 angstroms resolution: implications for atcase mutants and the mechanism of negative cooperativity

PDB Compounds: (D:) Aspartate carbamoyltransferase regulatory chain

SCOPe Domain Sequences for d1raad2:

Sequence; same for both SEQRES and ATOM records:

>d1raad2 g.41.7.1 (D:101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli [TaxId: 562]}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan

Timeline for d1raad2:

• d1raad2 first appeared (with stable ids) in SCOP 1.55
  
• d1raad2 appears in SCOPe 2.03
  
• d1raad2 appears in SCOPe 2.05
  
• d1raad2 appears in the current release, SCOPe 2.08