› 1e19

X-ray diffraction
1.5Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) ATP + carbamate = ADP + carbamoyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161158 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbamate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 314 amino acids
Theoretical weight: 34.48 KDa
Source organism: Pyrococcus furiosus
UniProt:
  • Canonical: P95474 (Residues: 1-314; Coverage: 100%)
Gene names: PF0676, cpa, cpkA
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

2 bound ligands:
Ligand ADP 2 x ADP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P212121
Unit cell:
a: 55.4Å b: 91.7Å c: 133.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.218

Quick links

Citations

2 review citations

Amino acid biosynthesis: new architectures in allosteric enzymes.
Curien et al. (2008)
1 more

10 mentions without citation

Sources and Fates of Carbamyl Phosphate: A Labile Energy-Rich Molecule with Multiple Facets.
Shi et al. (2018)
9 more