1acm

X-ray diffraction
2.8Å resolution

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

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-141554 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Aspartate carbamoyltransferase catalytic subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 310 amino acids
Theoretical weight: 34.25 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided
UniProt:
  • Canonical: P0A786 (Residues: 2-311; Coverage: 100%)
Gene names: JW4204, b4245, pyrB
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase
Aspartate carbamoyltransferase regulatory chain Chains: B, D
Molecule details ›
Chains: B, D
Length: 153 amino acids
Theoretical weight: 17.07 KDa
Source organism: Escherichia coli K-12
Expression system: Not provided
UniProt:
  • Canonical: P0A7F3 (Residues: 1-153; Coverage: 100%)
Gene names: JW4203, b4244, pyrI
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P321
Unit cell:
a: 122.2Å b: 122.2Å c: 156.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Not provided