8atc

X-ray diffraction
2.5Å resolution

COMPLEX OF N-PHOSPHONACETYL-L-ASPARTATE WITH ASPARTATE CARBAMOYLTRANSFERASE. X-RAY REFINEMENT, ANALYSIS OF CONFORMATIONAL CHANGES AND CATALYTIC AND ALLOSTERIC MECHANISMS

Released:
Source organism: Escherichia coli
Entry authors: Ke H, Lipscomb WN, Cho Y, Honzatko RB

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dodecamer (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: 34.34 KDa
Source organism: Escherichia coli
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
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: 122.11Å b: 122.11Å c: 156.17Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.165 not available not available
Expression system: Not provided