› 2air

X-ray diffraction
2Å resolution

T-state Active Site of Aspartate Transcarbamylase:Crystal Structure of the Carbamyl Phosphate and L-alanosine Ligated Enzyme

Released:
DOI: 10.2210/pdb2air/pdb
PDB entry 2air coloured by chain, front view.
PDB entry 2air coloured by chain, side view.
PDB entry 2air coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
T-state active site of aspartate transcarbamylase: crystal structure of the carbamyl phosphate and L-alanosine ligated enzyme.
Huang J, Lipscomb WN
Biochemistry 45 346-52 (2006)
PMID: 16401065

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, G
Molecule details ›
Chains: A, G
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, H
Molecule details ›
Chains: B, H
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 CP 2 x CP
Ligand AL0 2 x AL0
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: R3
Unit cell:
a: 129.152Å b: 129.152Å c: 198.097Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.239 0.273
Expression system: Escherichia coli

Quick links

Citations

1 review citation

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases.
Shi et al. (2015)
4 other articles

5 mentions without citation

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