› 2fzg

X-ray diffraction
2.25Å resolution

The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.25 Resolution

Released:
DOI: 10.2210/pdb2fzg/pdb
PDB entry 2fzg coloured by chain, front view.
PDB entry 2fzg coloured by chain, side view.
PDB entry 2fzg coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
T-state inhibitors of E. coli aspartate transcarbamoylase that prevent the allosteric transition.
Heng S, Stieglitz KA, Eldo J, Xia J, Cardia JP, Kantrowitz ER
Biochemistry 45 10062-71 (2006)
PMID: 16906764

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dodecamer (preferred)
Assembly name:
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: 34.34 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
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: 17.14 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7F3 (Residues: 1-153; Coverage: 100%)
Gene names: JW4203, b4244, pyrI
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand EOB 2 x EOB
Ligand ZN 2 x ZN
Ligand CTP 2 x CTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P321
Unit cell:
a: 119.94Å b: 119.94Å c: 141.97Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.201 0.237
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Understanding allosteric and cooperative interactions in enzymes.
Cornish-Bowden A. (2014)
1 more

3 mentions without citation

Allostery and cooperativity in Escherichia coli aspartate transcarbamoylase.
Kantrowitz ER. (2012)
2 more