SCOP 1.71: Domain d1acma1: 1acm A:1-150

Lineage for d1acma1 (1acm A:1-150)

1. Root: SCOP 1.71

2. Class c: Alpha and beta proteins (a/b) [51349] (134 folds)

3. Fold c.78: ATC-like [53670] (2 superfamilies)
   consists of two similar domains related by pseudo dyad; duplication
   core: 3 layers, a/b/a, parallel beta-sheet of 4 strands, order 2134

4. Superfamily c.78.1: Aspartate/ornithine carbamoyltransferase [53671] (1 family)

5. Family c.78.1.1: Aspartate/ornithine carbamoyltransferase [53672] (3 proteins)

6. Protein Aspartate carbamoyltransferase catalytic subunit [53673] (4 species)

7. Species Escherichia coli [TaxId:562] [53674] (36 PDB entries)

8. Domain d1acma1: 1acm A:1-150 [35180]
   Other proteins in same PDB: d1acmb1, d1acmb2, d1acmd1, d1acmd2

Details for d1acma1

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 d1acma1:

Sequence; same for both SEQRES and ATOM records:

>d1acma1 c.78.1.1 (A:1-150) Aspartate carbamoyltransferase catalytic subunit {Escherichia coli}
anplyqkhiisindlsrddlnlvlataaklkanpqpellkhkviascffeastatrlsfq
tsmhrlgasvvgfsdsantslgkkgetladtisvistyvdaivmrhpqegaarlatefsg
nvpvlnagdgsnqhptqtlldlftiqqteg

Timeline for d1acma1:

• d1acma1 first appeared (with stable ids) in SCOP 1.55
  
• d1acma1 appears in SCOP 1.69
  
• d1acma1 appears in SCOP 1.73
  
• d1acma1 appears in the current release, SCOPe 2.08