› 2we5

X-ray diffraction
1.39Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141077 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbamate kinase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 310 amino acids
Theoretical weight: 32.96 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A2X7 (Residues: 1-310; Coverage: 100%)
Gene names: EF_0106, arcC, arcC-1, arcC1
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

3 bound ligands:
Ligand ADP 3 x ADP
Ligand MG 3 x MG
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P3121
Unit cell:
a: 103.522Å b: 103.522Å c: 155.414Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.201 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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

4 mentions without citation

Chemical Composition, Antimicrobial Properties of Siparuna guianensis Essential Oil and a Molecular Docking and Dynamics Molecular Study of its Major Chemical Constituent.
Santana de Oliveira et al. (2020)
3 more