SCOP 1.71: Domain d1acmd2: 1acm D:101-153

Lineage for d1acmd2 (1acm D:101-153)

1. Root: SCOP 1.71

2. Class g: Small proteins [56992] (79 folds)

3. Fold g.41: Rubredoxin-like [57769] (14 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] (1 family)

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] (2 species)

7. Species Escherichia coli [TaxId:562] [57828] (33 PDB entries)

8. Domain d1acmd2: 1acm D:101-153 [45308]
   Other proteins in same PDB: d1acma1, d1acma2, d1acmb1, d1acmc1, d1acmc2, d1acmd1
   complexed with pal, zn; mutant

Details for d1acmd2

PDB Entry: 1acm, 2.8 Å

PDB Description: arginine 54 in the active site of escherichia coli aspartate transcarbamoylase is critical for catalysis: a site-specific mutagenesis, nmr and x-ray crystallography study

SCOP Domain Sequences for d1acmd2:

Sequence; same for both SEQRES and ATOM records:

>d1acmd2 g.41.7.1 (D:101-153) Aspartate carbamoyltransferase, Regulatory-chain, C-terminal domain {Escherichia coli}
eridnvlvcpnsncishaepvsssfavrkrandialkckycekefshnvvlan

Timeline for d1acmd2:

• d1acmd2 first appeared (with stable ids) in SCOP 1.55
  
• d1acmd2 appears in SCOP 1.69
  
• d1acmd2 appears in SCOP 1.73
  
• d1acmd2 appears in the current release, SCOPe 2.08